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
- 6A0A
- Type
- protein
- Length
- 89 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen type III peptide
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen type III peptide | protein | 29 | 0% helix, 0% strand | — |
| B, C | Collagen type III peptide | protein | 30 | 0% helix, 0% strand | — |
Interfaces
3 interfaces between chains.
- B–C · 974 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 948 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 902 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (hydroxylation).
Compared structures
- 6A0A · Structure of a triple-helix region of human collagen type III · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6A0A · PDBe 6A0A
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