MolNFT v1 · #148054 · protein
Crystal structure of an unlignaded peptide-substrate-binding domain of human type II collagen prolyl 4-hydroxylase
6EVL · Prolyl 4-hydroxylase subunit alpha-2: “Crystal structure of an unlignaded peptide-substrate-binding domain of human type II collagen prolyl…”. X-ray diffraction, 2 ligands (GLY, SO4). MolNFT v1 #148054 on GenesisL1: 3D structure…
- PDB
- 6EVL
- Type
- protein
- Length
- 94 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prolyl 4-hydroxylase subunit alpha-2
- EC
- 1.14.11.2
- UniProt
- O15460
- Ligands
- GLY, SO4
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl 4-hydroxylase subunit alpha-2 (EC 1.14.11.2) | protein | 94 | 76% helix, 0% strand | O15460 |
Ligands and binding sites
- GLY · Glycine · ligand · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EVL · Crystal structure of an unlignaded 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 0.93
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 6EVL · PDBe 6EVL · UniProt O15460
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