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The structure of human erythrocyte NADH-cytochrome B5 reductase

Analyse The structure of human erythrocyte NADH-cytochrome B5 reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UMK
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADH-cytochrome B5 reductase
EC: 1.6.2.2
UniProt: P00387
Ligands: FAD
Pockets: 2 · best druggability 0.64

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADH-cytochrome B5 reductase (EC 1.6.2.2)	protein	271	24% helix, 35% strand	P00387

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · 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	393	0.64	0.78	50	FAD
2	106	0.44	0.78	21	empty

Compared structures

1UMK · The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase · the same entry in another collection · chain A against A, TM-score 1.00
P00387 · AlphaFold monomer V2.0 prediction for NADH-cytochrome B5 reductase 3 (P00387) · 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 P00387
Elsewhere: RCSB PDB 1UMK · PDBe 1UMK · UniProt P00387

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