Research workbench

Human biliverdin IX beta reductase: NADP/BILIVERDIN IX alpha ternary complex

Analyse Human biliverdin IX beta reductase: NADP/BILIVERDIN IX alpha ternary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HE2
Type: protein
Length: 205 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Biliverdin IX beta reductase
EC: 1.3.1.24
UniProt: P30043
Ligands: NAP, BLA
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biliverdin IX beta reductase (EC 1.3.1.24)	protein	205	38% helix, 21% strand	P30043

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
BLA · Biliverdine IX alpha · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	505	0.72	0.81	44	NAP, BLA

Compared structures

1HE2 · Human biliverdin IX beta reductase: NADP/biliverdin IX alpha ternary complex · the same entry in another collection · chain A against A, TM-score 1.00
P30043 · AlphaFold monomer V2.0 prediction for flavin reductase (NADPH) (P30043) · 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 P30043
Elsewhere: RCSB PDB 1HE2 · PDBe 1HE2 · UniProt P30043

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