Research workbench
Structural basis of collagen stabilization induced by proline hydroxylation
Analyse Structural basis of collagen stabilization induced by proline hydroxylation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G9W
- Type
- protein
- Length
- 21 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen-like peptide
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen-like peptide | protein | 9 | 0% helix, 0% strand | — |
| B, C | Collagen-like peptide | protein | 6 | 0% helix, 0% strand | — |
Interfaces
3 interfaces between chains.
- A–B · 195 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 191 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 181 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1G9W · Structural basis of collagen stabilization induced by proline hydroxylation · 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 1G9W · PDBe 1G9W
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