MolNFT v1 · #176867 · protein
Trans-3/4-proline-hydroxylase H11 with akg and L-proline
7E07: “Trans-3/4-proline-hydroxylase H11 with akg and L-proline”. X-ray diffraction, 2 ligands (AKG, FE). MolNFT v1 #176867 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7E07
- Type
- protein
- Length
- 537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- S5TUM1
- Ligands
- AKG, FE
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 268 | — | S5TUM1 |
| B | — | protein | 269 | — | S5TUM1 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · 2 copies · chains A, B
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7E07 · Trans-3/4-proline-hydroxylase H11 with AKG and L-proline · the same entry in another collection · chain B against B, 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
- Every structure of UniProt S5TUM1
- Elsewhere: RCSB PDB 7E07 · PDBe 7E07 · UniProt S5TUM1
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