Research workbench
Structure of a triple-helix region of human collagen type III
Analyse Structure of a triple-helix region of human collagen type III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WWS
- Type
- protein
- Length
- 81 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen alpha-1(III) chain
- UniProt
- P02461
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Collagen alpha-1(III) chain | protein | 27 | 0% helix, 0% strand | P02461 |
Interfaces
3 interfaces between chains.
- B–C · 900 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 838 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 817 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (hydroxylation).
Compared structures
- 7WWS · Structure of a triple-helix region of human collagen type III from Trautec · the same entry in another collection · chain A against A, TM-score 1.00
- P02461 · AlphaFold monomer V2.0 prediction for collagen alpha-1(III) chain (P02461) · a predicted model of the same protein · chain C against A, TM-score 0.39
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P02461
- Elsewhere: RCSB PDB 7WWS · PDBe 7WWS · UniProt P02461
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