Research workbench
Crystal structure of the triple-helical collagen-like peptide, (pro- hyp-GLY)4-glu-lys-GLY(PRO-hyp-GLY)5
Analyse Crystal structure of the triple-helical collagen-like peptide, (pro… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QSU
- Type
- protein
- Length
- 89 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein ((pro-hyp-GLY)4- glu-lys-GLY(PRO-hyp-GLY)5)
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein ((pro-hyp-GLY)4- glu-lys-GLY(PRO-hyp-GLY)5) | protein | 30 | 0% helix, 0% strand | — |
| C | Protein ((pro-hyp-GLY)4- glu-lys-GLY(PRO-hyp-GLY)5) | protein | 29 | 0% helix, 0% strand | — |
Interfaces
3 interfaces between chains.
- A–B · 984 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 953 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 890 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 27 modified (hydroxylation).
Compared structures
- 1QSU · Crystal structure of the triple-helical collagen-like peptide… · 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 1QSU · PDBe 1QSU
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