MolNFT v1 · #129326 · protein

Crystal structure of amycolatopsis cytochrome P450 reductase gcob.

5OGX: “Crystal structure of amycolatopsis cytochrome P450 reductase gcob.”. X-ray diffraction, 4 ligands (FAD, FES, NA), 3 pockets (best druggability 0.68). MolNFT v1 #129326 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5OGX
Type: protein
Length: 333 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 reductase
UniProt: A0A076MZ01
Ligands: FAD, FES, NA, BR
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 reductase	protein	333	22% helix, 34% strand	A0A076MZ01

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
FES · Fe2/s2 (inorganic) cluster · ligand · chains A
NA · Sodium ion · metal · chains A
BR · Bromide ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	364	0.68	0.81	54	FAD
2	233	0.50	0.75	33	empty
3	52	0.26	0.74	16	empty

Compared structures

5OGX · Crystal structure of Amycolatopsis cytochrome P450 reductase GcoB. · the same entry in another collection · 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 A0A076MZ01
Elsewhere: RCSB PDB 5OGX · PDBe 5OGX · UniProt A0A076MZ01

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