Research workbench
Crystal structure of gzz shows up puckering of the proline ring in the xaa position.
Analyse Crystal structure of gzz shows up puckering of the proline ring in the xaa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YM8
- Type
- protein
- Length
- 162 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen gly-4(R)HYP-4(R)HYP
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, G, D, E, F | Collagen gly-4(R)HYP-4(R)HYP | protein | 27 | 0% helix, 0% strand | — |
Interfaces
15 interfaces between chains.
- D–E · 873 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 871 Ų buried · 10 hydrogen bonds · protein-protein
- B–G · 866 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 861 Ų buried · 9 hydrogen bonds · protein-protein
- A–G · 800 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 108 modified (hydroxylation).
Compared structures
- 1YM8 · crystal structure of GZZ shows up puckering of the proline ring 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 1YM8 · PDBe 1YM8
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