Research workbench
Crystal structure of a collagen-like peptide with 3(S)HYP in the xaa position
Analyse Crystal structure of a collagen-like peptide with 3(S)HYP in the xaa position in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G66
- Type
- protein
- Length
- 75 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen
- Ligands
- HY3
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen | protein | 24 | 0% helix, 0% strand | — |
| B | Collagen | protein | 25 | 0% helix, 0% strand | — |
| G | Collagen | protein | 26 | 0% helix, 0% strand | — |
Ligands and binding sites
- HY3 · 3-hydroxyproline · ligand · 6 copies · chains A, B, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- B–G · 810 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 790 Ų buried · 7 hydrogen bonds · protein-protein
- A–G · 746 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 26 modified, 12 covalent (hydroxylation, covalent ligand).
Compared structures
- 2G66 · Crystal structure of a collagen-like peptide with 3(S)Hyp in the Xaa position · the same entry in another collection · chain G against G, 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 2G66 · PDBe 2G66
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