MolNFT v1 · #13451 · protein

Structure of biliverdin reductase and the enzyme-NADH complex

1LC0: “Structure of biliverdin reductase and the enzyme-NADH complex”. X-ray diffraction, 1 ligand (PO4), 4 pockets (best druggability 0.65). MolNFT v1 #13451 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1LC0
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Biliverdin reductase a
EC: 1.3.1.24
UniProt: P46844
Ligands: PO4
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biliverdin reductase a (EC 1.3.1.24)	protein	290	41% helix, 28% strand	P46844

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A

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

Pockets

4 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	540	0.65	0.76	47	PO4
2	155	0.43	0.74	21	empty
3	85	0.39	0.77	17	empty
4	52	0.28	0.75	10	empty

Compared structures

1LC0 · Structure of Biliverdin Reductase and the Enzyme-NADH Complex · the same entry in another collection · chain A against A, TM-score 1.00
P46844 · AlphaFold monomer V2.0 prediction for biliverdin reductase a (P46844) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P46844
Elsewhere: RCSB PDB 1LC0 · PDBe 1LC0 · UniProt P46844

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.