MolNFT v1 · #110876 · protein

Rat cypor mutant - G143DEL

4Y9U · NADPH--cytochrome P450 reductase: “Rat cypor mutant - G143DEL”. X-ray diffraction, 4 ligands (FMN, FAD, NAP), 13 pockets (best druggability 0.81). MolNFT v1 #110876 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4Y9U
Type: protein
Length: 1,208 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADPH--cytochrome P450 reductase
EC: 1.6.2.4
UniProt: P00388
Ligands: FMN, FAD, NAP, PO4
Pockets: 13 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADPH--cytochrome P450 reductase (EC 1.6.2.4)	protein	608	38% helix, 20% strand	P00388
B	NADPH--cytochrome P450 reductase (EC 1.6.2.4)	protein	600	38% helix, 22% strand	P00388

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
PO4 · Phosphate ion · ion · chains B

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

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	475	0.81	0.88	74	empty
2	674	0.78	0.83	78	empty
3	381	0.69	0.81	32	NAP
4	372	0.68	0.81	36	NAP
5	245	0.61	0.81	44	FAD

Interfaces

1 interface between chains.

A–B · 719 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4Y9U · rat CYPOR mutant - G143del · the same entry in another collection · chain A against A, TM-score 1.00
P00388 · AlphaFold monomer V2.0 prediction for NADPH--cytochrome P450 reductase (P00388) · 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 P00388
Elsewhere: RCSB PDB 4Y9U · PDBe 4Y9U · UniProt P00388

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