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Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (R84A mutant)

Analyse Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (R84A mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZBY
Type: protein
Length: 400 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450-SU1
EC: 1.14.14.1
UniProt: P18326
Ligands: HEM
Pockets: 2 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450-SU1 (EC 1.14.14.1)	protein	400	52% helix, 9% strand	P18326

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	669	0.88	0.92	67	HEM
2	70	0.46	0.83	19	empty

Compared structures

2ZBY · Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (R84A mutant) · the same entry in another collection · chain A against A, TM-score 1.00
P18326 · AlphaFold monomer V2.0 prediction for vitamin D3 dihydroxylase (P18326) · a predicted model of the same protein · chain A against A, 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 P18326
Elsewhere: RCSB PDB 2ZBY · PDBe 2ZBY · UniProt P18326

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