8YV3: Collagen alpha-1 chain
The heterotrimer structure of peptides derived from human collagen type I. Determined by X-ray diffraction at 1.68 Å resolution. Released 2 Apr 2025.
- Method
- X-ray diffraction
- Resolution
- 1.68 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 1,564
- Mol. weight
- 17.64 kDa
- Released
- 2 Apr 2025
Explore 8YV3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8YV3 contains 13 α-helices and 0 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-8 | 7 | |
| α-helix | 10-23 | 14 | |
| α-helix | 25-29 | 5 | |
Chain B: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-8 | 7 | |
| α-helix | 10-29 | 20 | |
Chain C: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-11 | 9 | |
| α-helix | 13-29 | 17 | |
Chain D: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-11 | 10 | |
| α-helix | 13-29 | 17 | |
Chain E: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-18 | 17 | |
| α-helix | 20-29 | 10 | |
Chain F: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-14 | 13 | |
| α-helix | 16-29 | 14 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Collagen alpha-1(I) chain | A, D | protein | 31 | Homo sapiens | P02452 (AlphaFold model) |
| Collagen alpha-2(I) chain | B, C, E, F | protein | 31 | Homo sapiens | P08123 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>8YV3_1 Collagen alpha-1(I) chain (chains A, D)
XPVGARGPAGPQGPRGDKGETGEQGDRGIKG
Sequence of entity 2 (B, C, E, F), FASTA
>8YV3_2 Collagen alpha-2(I) chain (chains B, C, E, F)
XAVGPRGPSGPQGIRGDKGEPGEKGPRGLPG
Primary citation
The heterotrimer structure of peptides derived from human collagen type I. Zhu, Y., Yang, X., Sun, F. To be published.
Other PDB entries of the same protein (UniProt P02452 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5CTD 1.6 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…
- 1Q7D 1.8 Å, Structure of the integrin alpha2beta1 binding collagen peptide
- 5CTI 1.9 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…
- 5CVA 2.1 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…
- 3EJH 2.1 Å, Crystal Structure of the Fibronectin 8-9FnI Domain Pair in Complex with a Type-I…
- 5K31 2.2 Å, Crystal structure of Human fibrillar procollagen type I C-propeptide Homo-trimer
- 5CVB 2.25 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…
- 5OU8 2.5 Å, Crystal structure of Glycoprotein VI in complex with collagen-peptide (GPO)5
- 5OU9 2.5 Å, Crystal structure of Glycoprotein VI in complex with collagen-peptide (GPO)3
- 3GXE 2.6 Å, Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair
- 7E7B 2.6 Å, Cryo-EM structure of the SARS-CoV-2 furin site mutant S-Trimer from a subunit vaccine…
- 7E7D 3.2 Å, Cryo-EM structure of the SARS-CoV-2 wild-type S-Trimer from a subunit vaccine candidate
Browse structure collections
About this viewer
MolViewer shows 8YV3 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.