Homo sapiens · seed P69905 · 142 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P69905 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 1.10.490.10 SCOP 8039586 SCOP 8036374 SCOP 8036375 SCOP 8039836 SCOP 8039587 SCOP 8039838 SCOP 8042195 SCOP 8042196 RCSB 1GLI 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.
1GLI, 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.
245 distinct constructs across 533 entries. 734 polymer entities differ from the UniProt canonical sequence in some way, 0 carry a recognised expression tag and 0 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 |
|---|---|---|---|---|
| 248 | 141 | 1.25 | 1IRD | residues 2-142 |
| 196 | 146 | 1.25 | 1IRD | residues 2-147 |
| 30 | 142 | 1.59 | 1BZ1 | matches the canonical sequence |
| 27 | 147 | 1.70 | 1DXT | matches the canonical sequence |
| 20 | 146 | 1.45 | 2D5X | matches the canonical sequence |
| 17 | 145 | 1.85 | 5E29 | residues 3-147 |
| 15 | 145 | 1.34 | 6II1 | matches the canonical sequence |
| 12 | 141 | 1.60 | 1NS9 | residues 2-142; N83D, D86N |
| 12 | 143 | 1.30 | 2H8F | matches the canonical sequence |
| 12 | 146 | 1.30 | 2H8F | residues 2-147 |
| 11 | 140 | 1.92 | 4MQI | residues 2-141 |
| 11 | 141 | 1.75 | 2QSS | residues 2-142 |
| 11 | 146 | 1.40 | 6KAO | residues 2-147; E7K |
| 10 | 139 | 2.20 | 6HAL | residues 3-141 |
| 9 | 146 | 1.70 | 1DXU | residues 2-147; V2M |
| 9 | 146 | 1.76 | 5E6E | residues 2-147; E7V |
| 6 | 140 | 3.10 | 9S3P | residues 3-142 |
| 6 | 143 | 1.80 | 2AA1 | matches the canonical sequence |
| 6 | 146 | 0.91 | 3QM5 | matches the canonical sequence |
| 6 | 146 | 1.25 | 3D1K | matches the canonical sequence |
| 6 | 146 | 1.39 | 6ZMX | matches the canonical sequence |
| 5 | 142 | 2.20 | 8WIZ | matches the canonical sequence |
| 5 | 146 | 1.80 | 1C7C | residues 2-147; V2M, N109K |
| 5 | 146 | 2.20 | 8WIZ | matches the canonical sequence |
| 4 | 141 | 1.07 | 2W72 | residues 2-142; V2M, L30Y, H59Q |
Showing the 25 most-used of 245.
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 |
|---|---|---|---|
| tetrameric | 4 | 465 | 87.2% |
| trimeric | 3 | 15 | 2.8% |
| dimeric | 2 | 14 | 2.6% |
| monomeric | 1 | 12 | 2.3% |
| hexameric | 6 | 12 | 2.3% |
| pentameric | 5 | 5 | 0.9% |
| heptameric | 7 | 5 | 0.9% |
| decameric | 10 | 3 | 0.6% |
387 entries have the depositor's assembly corroborated by PISA, 142 carry the depositor's word alone and 4 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 14 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1QXD, 1QXE, 1SDK, 1SDL, 1UC3, 1Z8U, 2ZLT, 2ZLV, 3A59, 3CY5, 3DHR, 3GYS, 8DOV, 9JYU.
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 |
|---|---|---|---|
| Globins | CATH 1.10.490.10 | 2–142 | 870 |
| Globin-like | SCOP2B 8039586 | 2–142 | 20 |
| Globin-like | SCOP2B 8036374 | 2–142 | 13 |
| Globin-like | SCOP2B 8036375 | 2–142 | 13 |
| Globin-like | SCOP2B 8039836 | 3–142 | 356 |
| Globin-like | SCOP2B 8039587 | 3–142 | 20 |
| Globin-like | SCOP2B 8039838 | 4–142 | 340 |
| Globin-like | SCOP2B 8042195 | 4–142 | 11 |
| Globin-like | SCOP2B 8042196 | 24–142 | 11 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| HEM | cofactor | Protoporphyrin Ix Containing Fe | 526 | 0.91 |
| CMO | solvent | Carbon Monoxide | 129 | 0.96 |
| OXY | solvent | Oxygen Molecule | 73 | 0.91 |
| SO4 | ion | Sulfate Ion | 39 | 0.95 |
| PO4 | ion | Phosphate Ion | 23 | 1.07 |
| GOL | cryoprotectant | Glycerol | 22 | 1.09 |
| HNI | ligand | Protoporphyrin Ix Containing Ni(Ii) | 18 | 1.40 |
| NAG | cofactor | 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose | 13 | 2.80 |
| 2FU | ligand | But-2-Enedial | 12 | 1.40 |
| MBN | ligand | Toluene | 12 | 1.25 |
| CA | ion | Calcium Ion | 12 | 2.64 |
| EDO | cryoprotectant | 1,2-Ethanediol | 10 | 0.91 |
| CYN | ion | Cyanide Ion | 9 | 0.91 |
| NO | solvent | Nitric Oxide | 8 | 0.95 |
| ACE | ligand | Acetyl Group | 5 | 1.25 |
| NO2 | ion | Nitrite Ion | 5 | 1.80 |
| O4B | ligand | 1,4,7,10,13,16-Hexaoxacyclooctadecane | 5 | 1.48 |
| DG2 | ligand | (2r)-2,3-Diphosphoglyceric Acid | 4 | 1.80 |
| NA | ion | Sodium Ion | 3 | 1.39 |
| CL | ion | Chloride Ion | 3 | 2.10 |
Parsed from the free text 382 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 424
entries that recorded anything at all.
Median pH 7.0
(range 4.0 to 9.5).
530 entries carry a wwPDB validation report: 231 clean, 159 worth a check and 140 with something to explain. Median clashscore 7.2, median RSRZ outliers 1.57%, median R-free minus R-work 0.046. 455 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 365 | 1.07 | 719 | 100% |
| Equus caballus | 21 | 1.45 | 42 | 99% |
| Bos taurus | 16 | 1.34 | 28 | 99% |
| Trematomus bernacchii | 12 | 1.30 | 24 | 99% |
| Trematomus newnesi | 7 | 1.25 | 14 | 99% |
| Meleagris gallopavo | 6 | 1.39 | 12 | 100% |
| Alligator mississippiensis | 5 | 2.20 | 10 | 100% |
| Thunnus atlanticus | 9 | 0.91 | 9 | 71% |
| Oncorhynchus mykiss | 4 | 1.35 | 8 | 99% |
| Perca flavescens | 4 | 1.90 | 8 | 99% |
| Felis catus | 4 | 2.00 | 8 | 99% |
| Columba livia | 3 | 1.44 | 6 | 100% |
142 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 | Oxidative Characteristics of Turkey Hemoglobin A Containing Covalently Bound Epigallocatechin Gallate. J.Agric.Food Chem. doi:10.1021/acs.jafc.5c17482 |
| 2026 | Recombinant Hemoglobin rHb0.1 with Cross-Linked Alpha Subunits Preferentially Crystallizes in the beta 4 Oligomeric State, Potentially Driven by a beta G18(H116I) Mutation. Acs Omega doi:10.1021/acsomega.5c11376 |
| 2026 | Structural basis for hemoglobin scavenging by CD163 reveals mechanism of ligand promiscuity. Plos Biol. doi:10.1371/journal.pbio.3003788 |
| 2026 | Refining the mechanism of heme acquisition from free hemoglobin by Staphylococcus aureus IsdH. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2601134123 |
| 2026 | Hemoglobin's alpha-Helix-to-beta-Sheet Transition Enables Targeted mRNA Delivery to the Lung. Adv Sci doi:10.1002/advs.76092 |
| 2026 | Structural Basis of Hemoglobin Amyloid Fibrils Revealed by cryo-EM and Molecular Dynamics Simulations. Nano Lett. doi:10.1021/acs.nanolett.6c02217 |
| 2025 | Molecular basis of hemoglobin binding and heme removal in Corynebacterium diphtheriae. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2411833122 |
| 2025 | Base editing HbS to HbG-Makassar improves hemoglobin function supporting its use in sickle cell disease. Nat Commun doi:10.1038/s41467-025-56578-3 |
| 2025 | Conformational analysis of liganded human hemoglobin by cryo electron microscopy Biorxiv doi:10.1101/2025.07.07.661630 |
| 2025 | Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification. Nat Commun doi:10.1038/s41467-025-58243-1 |
| 2025 | Scavenger receptor CD163 multimerises to allow uptake of diverse ligands. Nat Commun doi:10.1038/s41467-025-62054-9 |
| 2025 | Calcium-dependent oligomerization of scavenger receptor CD163 facilitates the endocytosis of ligands. Nat Commun doi:10.1038/s41467-025-62013-4 |
| 2025 | Hemoglobin receptor redundancy in Staphylococcus aureus : molecular flexibility as a determinant of divergent hemophore activity. J Struct Biol X doi:10.1016/j.yjsbx.2025.100138 |
| 2025 | Structural elucidation of the haptoglobin-hemoglobin clearance mechanism by macrophage scavenger receptor CD163. Plos Biol. doi:10.1371/journal.pbio.3003264 |
| 2024 | Improving Protein Expression, Stability, and Function with ProteinMPNN. J.Am.Chem.Soc. doi:10.1021/jacs.3c10941 |
| 2024 | The structure of a haemoglobin-nanobody complex reveals human beta-subunit-specific interactions. Febs Lett. doi:10.1002/1873-3468.14958 |
| 2024 | The unique allosteric property of crocodilian haemoglobin elucidated by cryo-EM. Nat Commun doi:10.1038/s41467-024-49947-x |
| 2024 | The Cryo-EM structure of human CD163 bound to haptoglobin-hemoglobin reveals molecular mechanisms of hemoglobin scavenging. Nat Commun doi:10.1038/s41467-024-55171-4 |
| 2023 | Structural and oxidative investigation of a recombinant high-yielding fetal hemoglobin mutant. Front Mol Biosci doi:10.3389/fmolb.2023.1133985 |
| 2023 | Crystal structural investigations of heme protein derivatives resulting from reactions of aryl- and alkylhydroxylamines with human hemoglobin. J.Inorg.Biochem. doi:10.1016/j.jinorgbio.2023.112304 |
| 2023 | Anaerobic fixed-target serial crystallography using sandwiched silicon nitride membranes. Acta Crystallogr D Struct Biol doi:10.1107/S205979832300880X |
| 2023 | Protein-to-structure pipeline for ambient-temperature crystallography at VMXi Iucrj doi:10.1107/S2052252523003810 |
| 2023 | GBT021601 improves red blood cell health and the pathophysiology of sickle cell disease in a murine model. Br.J.Haematol. doi:10.1111/bjh.18771 |
| 2023 | The Shr receptor from Streptococcus pyogenes uses a cap and release mechanism to acquire heme-iron from human hemoglobin. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2211939120 |
| 2023 | Uniform thin ice on ultraflat graphene for high-resolution cryo-EM. Nat.Methods doi:10.1038/s41592-022-01693-y |
| 2022 | Design, Synthesis, and Antisickling Investigation of a Nitric Oxide-Releasing Prodrug of 5HMF for the Treatment of Sickle Cell Disease. Biomolecules doi:10.3390/biom12050696 |
| 2022 | Design, Synthesis, and Investigation of Novel Nitric Oxide (NO)-Releasing Aromatic Aldehydes as Drug Candidates for the Treatment of Sickle Cell Disease. Molecules doi:10.3390/molecules27206835 |
| 2022 | Cryo-EM structures of staphylococcal IsdB bound to human hemoglobin reveal the process of heme extraction. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2116708119 |
| 2021 | Structural studies of hemoglobin from two flightless birds, ostrich and turkey: insights into their differing oxygen-binding properties. Acta Crystallogr D Struct Biol doi:10.1107/S2059798321003417 |
| 2021 | PF-07059013: A Noncovalent Modulator of Hemoglobin for Treatment of Sickle Cell Disease. J.Med.Chem. doi:10.1021/acs.jmedchem.0c01518 |
| 2021 | MetAP2 inhibition modifies hemoglobin S to delay polymerization and improves blood flow in sickle cell disease. Blood Adv doi:10.1182/bloodadvances.2020003670 |
| 2021 | Effect of X-ray free-electron laser-induced shockwaves on haemoglobin microcrystals delivered in a liquid jet. Nat Commun doi:10.1038/s41467-021-21819-8 |
| 2021 | Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans. Acta Crystallogr.,Sect.F doi:10.1107/S2053230X2100306X |
| 2021 | A cryo-electron microscopy support film formed by 2D crystals of hydrophobin HFBI. Nat Commun doi:10.1038/s41467-021-27596-8 |
| 2020 | Direct observation of ligand migration within human hemoglobin at work. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.1913663117 |
| 2020 | Biodistribution PET/CT Study of Hemoglobin-DFO-89Zr Complex in Healthy and Lung Tumor-Bearing Mice. Int J Mol Sci doi:10.3390/ijms21144991 |
| 2020 | Exploration of Structure-Activity Relationship of Aromatic Aldehydes Bearing Pyridinylmethoxy-Methyl Esters as Novel Antisickling Agents. J.Med.Chem. doi:10.1021/acs.jmedchem.0c01287 |
| 2020 | VZHE-039, a novel antisickling agent that prevents erythrocyte sickling under both hypoxic and anoxic conditions. Sci Rep doi:10.1038/s41598-020-77171-2 |
| 2020 | The nitrosoamphetamine metabolite is accommodated in the active site of human hemoglobin: Spectroscopy and crystal structure. J.Inorg.Biochem. doi:10.1016/j.jinorgbio.2020.111262 |
| 2020 | Genetically engineered haemoglobin wrapped covalently with human serum albumins as an artificial O2carrier. J Mater Chem B doi:10.1039/c9tb02184a |