MolNFT v1 · #120051 · protein
Cytochrome P450 vdh (CYP107BR1) F106V mutant
5GNL · Vitamin D(3) 25-hydroxylase: “Cytochrome P450 vdh (CYP107BR1) F106V mutant”. X-ray diffraction, 1 ligand (HEM), 2 pockets (best druggability 0.78). MolNFT v1 #120051 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5GNL
- Type
- protein
- Length
- 395 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vitamin D(3) 25-hydroxylase
- EC
- 1.14.15.15
- UniProt
- C4B644
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vitamin D(3) 25-hydroxylase (EC 1.14.15.15) | protein | 395 | 50% helix, 9% strand | C4B644 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 793 | 0.78 | 0.81 | 75 | HEM, PG0 |
| 2 | 110 | 0.46 | 0.79 | 16 | empty |
Compared structures
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 C4B644
- Elsewhere: RCSB PDB 5GNL · PDBe 5GNL · UniProt C4B644
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