Homo sapiens · seed P13569 · 1480 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P13569 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.40.50.300 CATH 2.40.50.140 CATH 2.40.50.100 CATH 1.20.1560.10 SCOP 8033774 SCOP 8056723 SCOP 8057787 SCOP 8018329 SCOP 8018333 SCOP 8057792 SCOP 8057830 RCSB 6WBS PDBe
CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.
Every figure here is counted over the whole family rather than quoted from one entry.
6WBS, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.
How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.
91 distinct constructs across 237 entries. 177 polymer entities differ from the UniProt canonical sequence in some way, 43 carry a recognised expression tag and 3 carry a fusion partner.
"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.
| Entities | Length | Best (Å) | Best entry | What was made |
|---|---|---|---|---|
| 15 | 229 | 1.70 | 2PZE | residues 386-646; 1 internal deletion; N386S, V470M |
| 15 | 1325 | 2.84 | 8XOK | matches the canonical sequence |
| 10 | 573 | 2.77 | 7ZDG | matches the canonical sequence |
| 9 | 599 | 2.50 | 8SCB | matches the canonical sequence |
| 7 | 1480 | 2.10 | 9MXL | E1371Q |
| 6 | 286 | 2.20 | 1R0W | residues 388-673; M388S |
| 6 | 573 | 2.71 | 7ZDT | E500Q |
| 6 | 681 | 2.90 | 8FHK | His6; C154A, C256A, C351A +1 more |
| 5 | 558 | 2.79 | 7MSM | matches the canonical sequence |
| 5 | 584 | 2.82 | 9XNP | His8 |
| 5 | 584 | 2.93 | 8XSR | residues 1-580; 2 internal deletions; 2-residue insertion after 460; L3W, H9Y, I10V +172 more |
| 5 | 842 | 3.40 | 7DNY | matches the canonical sequence |
| 5 | 1325 | 2.70 | 8SX7 | 1 internal deletion; M1R, D2N, C3A +6 more |
| 4 | 28 | 1.76 | 7QI1 | residues 747-774 |
| 4 | 207 | 2.86 | 7F04 | matches the canonical sequence |
| 4 | 306 | 2.00 | 3NH6 | Thrombin site; residues 547-842; F547M, T549S, Y550S +7 more |
| 4 | 353 | 1.65 | 1OXS | matches the canonical sequence |
| 4 | 586 | 2.40 | 7P7Q | no UniProt reference for this entity, so it cannot be diffed against a canonical sequence |
| 4 | 595 | 3.00 | 6YAL | residues 4-598; V538I |
| 4 | 681 | 2.96 | 8T1P | His6 |
| 4 | 739 | 3.40 | 7N58 | His6 |
| 4 | 1479 | 2.80 | 8EIO | 1 internal deletion; E1371Q |
| 4 | 1480 | 3.80 | 9DW5 | matches the canonical sequence |
| 3 | 261 | 2.49 | 6GJQ | residues 386-646; N386S, V470M, S492P +2 more |
| 3 | 590 | 2.70 | 9IQG | residues 1-580; 2 internal deletions; 2-residue insertion after 460; L3W, H9Y, I10V +172 more |
Showing the 25 most-used of 91.
Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".
| Oligomeric state | Chains | Entries | Share |
|---|---|---|---|
| monomeric | 1 | 96 | 40.5% |
| dimeric | 2 | 85 | 35.9% |
| trimeric | 3 | 9 | 3.8% |
| 87-meric | 87 | 7 | 3.0% |
| hexameric | 6 | 7 | 3.0% |
| tetrameric | 4 | 4 | 1.7% |
| 55-meric | 55 | 4 | 1.7% |
| 88-meric | 88 | 3 | 1.3% |
75 entries have the depositor's assembly corroborated by PISA, 160 carry the depositor's word alone and 2 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 11 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1Q3H, 1R0W, 1R0X, 1R0Y, 1R0Z, 1R10, 1XF9, 1XMI, 2PZF, 3GD7, 3SI7.
Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.
| Domain | Source | Span (seed) | Chains |
|---|---|---|---|
| P-loop containing nucleotide triphosphate hydrolases | CATH 3.40.50.300 | 412–670 | 86 |
| Nucleic acid-binding proteins | CATH 2.40.50.140 | 737–781 | 4 |
| RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain | CATH 2.40.50.100 | 783–793 | 8 |
| ABC transporter type 1, transmembrane domain | CATH 1.20.1560.10 | 1229–1480 | 7 |
| Protein kinase-like (PK-like) | SCOP2B 8033774 | 15–351 | 2 |
| ABC transporter-like P-loop ATPases | SCOP2B 8056723 | 389–627 | 44 |
| ABC transporter-like P-loop ATPases | SCOP2B 8057787 | 390–628 | 8 |
| ABC transporter-like P-loop ATPases | SCOP2B 8018329 | 441–663 | 3 |
| MOP-like | SCOP2B 8018333 | 683–792 | 3 |
| ABC transporter-like P-loop ATPases | SCOP2B 8057792 | 1207–1426 | 20 |
| ABC transporter transmembrane region-like | SCOP2B 8057830 | 1231–1480 | 4 |
ATP84 entries
ADP29 entries
ANP24 entries
SF416 entries
POV15 entries
HEM6 entries
HT16 entries
HEB6 entries
VX85 entries
GTP4 entries
SCM4 entries
PUT4 entries
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| MG | ion | Magnesium Ion | 137 | 1.50 |
| ATP | cofactor | Adenosine-5'-Triphosphate | 84 | 1.50 |
| ADP | cofactor | Adenosine-5'-Diphosphate | 29 | 2.10 |
| ANP | cofactor | Phosphoaminophosphonic Acid-Adenylate Ester | 24 | 1.95 |
| ZN | ion | Zinc Ion | 21 | 2.40 |
| SF4 | ligand | Iron/sulfur Cluster | 16 | 2.50 |
| CLR | lipid/detergent | Cholesterol | 16 | 2.70 |
| POV | ligand | (2s)-3-(Hexadecanoyloxy)-2-[(9z)-Octadec-9-Enoyloxy]propyl 2-(Tr | 15 | 2.90 |
| ACY | cryoprotectant | Acetic Acid | 8 | 2.20 |
| CL | ion | Chloride Ion | 7 | 1.80 |
| VO4 | ion | Vanadate Ion | 7 | 2.70 |
| Y01 | lipid/detergent | Cholesterol Hemisuccinate | 6 | 2.90 |
| HEM | cofactor | Protoporphyrin Ix Containing Fe | 6 | 2.86 |
| HT1 | ligand | 2'-(4-Ethoxyphenyl)-5-(4-Methyl-1-Piperazinyl)-2,5'-Bi-Benzimida | 6 | 3.06 |
| D12 | lipid/detergent | Dodecane | 6 | 2.70 |
| HEB | cofactor | Heme B/c | 6 | 2.77 |
| GOL | cryoprotectant | Glycerol | 5 | 1.80 |
| SO4 | ion | Sulfate Ion | 5 | 1.80 |
| K | ion | Potassium Ion | 5 | 2.40 |
| VX8 | ligand | Lumacaftor | 5 | 2.70 |
Parsed from the free text 69 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 69
entries that recorded anything at all.
Median pH 7.5
(range 4.5 to 9.5).
237 entries carry a wwPDB validation report: 180 clean, 33 worth a check and 24 with something to explain. Median clashscore 6.31, median RSRZ outliers 4.35%, median R-free minus R-work 0.043. 237 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 117 | 1.50 | 92 | 100% |
| Escherichia coli K-12 | 25 | 2.71 | 20 | 24% |
| Oryctolagus cuniculus | 16 | 2.50 | 13 | 10% |
| Mycolicibacterium smegmatis MC2 155 | 12 | 2.70 | 8 | 15% |
| Bacillus subtilis subsp. subtilis str. 168 | 10 | 2.90 | 10 | 14% |
| Mus musculus | 9 | 2.20 | 8 | 19% |
| Escherichia coli BL21(DE3) | 6 | 2.86 | 5 | 24% |
| Saccharolobus solfataricus | 5 | 1.45 | 2 | 9% |
| Bos taurus | 5 | 2.70 | 3 | 97% |
| Mycobacterium tuberculosis H37Rv | 5 | 2.79 | 5 | 10% |
| Arabidopsis thaliana | 4 | 3.40 | 3 | 16% |
| Unknown | 4 | 0 | 2% |
1480 residues, numbered every ten. Every identity figure in this document is measured against this sequence.
active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions
Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.
One record per paper, not per entry.
| Year | Citation |
|---|---|
| 2026 | Molecular architecture and diversity of StopGo/2A translational recoding. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2528667123 |
| 2026 | Conformational Snapshots of CydDC in a Native Lipid Bilayer Coupling Heme Transport to Antibiotic Resistance. Adv Sci doi:10.1002/advs.76081 |
| 2026 | Mechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide. Sci Adv doi:10.1126/sciadv.aec5067 |
| 2026 | Cryo-EM structures of human ABCB7 reveal the molecular basis of mitochondrial matrix heme export. Commun Biol doi:10.1038/s42003-026-10223-x |
| 2025 | Structure of CFTR bound to (R)-BPO-27 unveils a pore-blockage mechanism. Nat Commun doi:10.1038/s41467-025-62199-7 |
| 2025 | Structure and mechanism of a mycobacterial isoniazid efflux pump MsRv1273c/72c with a degenerate nucleotide-binding site. Nat Commun doi:10.1038/s41467-025-59300-5 |
| 2025 | Programmable initiation of mRNA translation by trans-RNA. Nat.Biotechnol. doi:10.1038/s41587-025-02897-1 |
| 2025 | Structural basis for the reversal of human MRP4-mediated multidrug resistance by lapatinib. Cell Rep doi:10.1016/j.celrep.2025.115466 |
| 2025 | Structural basis of human ABCC4 recognition of cAMP and ligand recognition flexibility. Cell Biosci doi:10.1186/s13578-025-01377-y |
| 2025 | Drug-bound outward-facing conformation of a heterodimeric ABC exporter suggests a putative mechanism of drug translocation. Nat Commun doi:10.1038/s41467-025-65318-6 |
| 2024 | The eRF1 degrader SRI-41315 acts as a molecular glue at the ribosomal decoding center. Nat.Chem.Biol. doi:10.1038/s41589-023-01521-0 |
| 2024 | Structural basis of prostaglandin efflux by MRP4. Nat.Struct.Mol.Biol. doi:10.1038/s41594-023-01176-4 |
| 2024 | Structural basis for CFTR inhibition by CFTR inh -172. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2316675121 |
| 2024 | The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2409049121 |
| 2024 | The ATP-bound inward-open conformation of ABCC4 reveals asymmetric ATP binding for substrate transport. Febs Lett. doi:10.1002/1873-3468.14955 |
| 2024 | The role of ATP-binding Cassette subfamily B member 6 in the inner ear. Nat Commun doi:10.1038/s41467-024-53663-x |
| 2024 | N 6 -methyladenosine in 5' UTR does not promote translation initiation. Mol.Cell doi:10.1016/j.molcel.2023.12.028 |
| 2024 | Cryo-EM structure of cadmium-bound human ABCB6. Commun Biol doi:10.1038/s42003-024-06377-1 |
| 2024 | Allosteric inhibition of CFTR gating by CFTRinh-172 binding in the pore. Nat Commun doi:10.1038/s41467-024-50641-1 |
| 2024 | Structure-based discovery of CFTR potentiators and inhibitors. Cell doi:10.1016/j.cell.2024.04.046 |
| 2023 | Dissecting the conformational complexity and mechanism of a bacterial heme transporter. Nat.Chem.Biol. doi:10.1038/s41589-023-01314-5 |
| 2023 | Structure of an endogenous mycobacterial MCE lipid transporter. Nature doi:10.1038/s41586-023-06366-0 |
| 2023 | Cryo-EM structures of mitochondrial ABC transporter ABCB10 in apo and biliverdin-bound form. Nat Commun doi:10.1038/s41467-023-37851-9 |
| 2023 | Asymmetric conformations and lipid interactions shape the ATP-coupled cycle of a heterodimeric ABC transporter. Nat Commun doi:10.1038/s41467-023-42937-5 |
| 2023 | Structural basis for substrate and inhibitor recognition of human multidrug transporter MRP4. Commun Biol doi:10.1038/s42003-023-04935-7 |
| 2023 | Structural and mechanistic basis of substrate transport by the multidrug transporter MRP4. Structure doi:10.1016/j.str.2023.08.014 |
| 2023 | Cryo-EM structure ofABCC4 Nat Cardiovasc Res |
| 2023 | Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation. Nat Commun doi:10.1038/s41467-023-40881-y |
| 2023 | Cryo-EM structures of a prokaryotic heme transporter CydDC. Protein Cell doi:10.1093/procel/pwad022 |
| 2023 | W546 stacking disruption traps the human porphyrin transporter ABCB6 in an outward-facing transient state. Commun Biol doi:10.1038/s42003-023-05339-3 |
| 2023 | CFTR function, pathology and pharmacology at single-molecule resolution. Nature doi:10.1038/s41586-023-05854-7 |
| 2022 | Macrocycle-stabilization of its interaction with 14-3-3 increases plasma membrane localization and activity of CFTR. Nat Commun doi:10.1038/s41467-022-31206-6 |
| 2022 | Structural basis for PoxtA-mediated resistance to phenicol and oxazolidinone antibiotics. Nat Commun doi:10.1038/s41467-022-29274-9 |
| 2022 | Mechanism of CFTR correction by type I folding correctors. Cell doi:10.1016/j.cell.2021.12.009 |
| 2022 | Interplay between an ATP-binding cassette F protein and the ribosome from Mycobacterium tuberculosis. Nat Commun doi:10.1038/s41467-022-28078-1 |
| 2022 | Molecular structures reveal synergistic rescue of Delta 508 CFTR by Trikafta modulators. Science doi:10.1126/science.ade2216 |
| 2022 | Structures of the CcmABCD heme release complex at multiple states. Nat Commun doi:10.1038/s41467-022-34136-5 |
| 2022 | Cryo-EM structure of AMP-PNP-bound human mitochondrial ATP-binding cassette transporter ABCB7. J.Struct.Biol. doi:10.1016/j.jsb.2022.107832 |
| 2022 | Structural Insights into Porphyrin Recognition by the Human ATP-Binding Cassette Transporter ABCB6. Mol.Cells doi:10.14348/molcells.2022.0040 |
| 2022 | Glutathione binding to the plant At Atm3 transporter and implications for the conformational coupling of ABC transporters. Elife doi:10.7554/eLife.76140 |