Research workbench
Crystal structure of a pro-9 complexed peptide-substrate-binding domain of human type II collagen prolyl 4-hydroxylase
Analyse Crystal structure of a pro-9 complexed peptide-substrate-binding domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EVM
- Type
- protein
- Length
- 104 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prolyl 4-hydroxylase subunit alpha-2; Pro-9
- EC
- 1.14.11.2
- UniProt
- O15460
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl 4-hydroxylase subunit alpha-2 (EC 1.14.11.2) | protein | 95 | 75% helix, 0% strand | O15460 |
| C | Pro-9 | protein | 9 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 445 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6EVM · Crystal structure of a Pro-9 complexed peptide-substrate-binding domain of human type II… · the same entry in another collection · chain A against A, TM-score 1.00
- O15460 · AlphaFold monomer V2.0 prediction for prolyl 4-hydroxylase subunit alpha-2 (O15460) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O15460
- Elsewhere: RCSB PDB 6EVM · PDBe 6EVM · UniProt O15460
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