Research workbench
Crystal structure of the collagen triple helix model [{pro-HYP(R)- GLY}4-{HYP(S)-pro-GLY}2-{pro-HYP(R)-GLY}4]3
Analyse Crystal structure of the collagen triple helix model [{pro-HYP(R)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B2C
- Type
- protein
- Length
- 270 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen-like peptide
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I | Collagen-like peptide | protein | 30 | 0% helix, 0% strand | — |
Interfaces
27 interfaces between chains.
- B–C · 940 Ų buried · 11 hydrogen bonds · protein-protein
- H–I · 938 Ų buried · 10 hydrogen bonds · protein-protein
- G–H · 936 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 929 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 926 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 90 modified (hydroxylation, nonstandard).
Compared structures
- 3B2C · Crystal structure of the collagen triple helix model… · 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 3B2C · PDBe 3B2C
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