MolNFT v1 · #120282 · protein

Structure of NADH-cytochrome B5 reductase refined with the multipolar atomic model at 0.78A

5GV8 · NADH-cytochrome B5 reductase 3: “Structure of NADH-cytochrome B5 reductase refined with the multipolar atomic model at 0.78A”. X-ray diffraction, 1 ligand (FAD), 3 pockets (best druggability 0.68). MolNFT v1 #120282 on GenesisL1: 3D…

PDB: 5GV8
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADH-cytochrome B5 reductase 3
EC: 1.6.2.2
UniProt: P83686
Ligands: FAD
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADH-cytochrome B5 reductase 3 (EC 1.6.2.2)	protein	272	24% helix, 35% strand	P83686

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
GOL · Glycerol · additive · 4 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	529	0.68	0.78	51	FAD, GOL
2	109	0.41	0.77	22	empty
3	50	0.29	0.75	19	empty

Compared structures

P83686 · AlphaFold monomer V2.0 prediction for NADH-cytochrome B5 reductase 3 (P83686) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P83686
Elsewhere: RCSB PDB 5GV8 · PDBe 5GV8 · UniProt P83686

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