MolNFT v1 · #129061 · protein

Binary complex of catharanthus roseus vitrosamine synthase with NADP+

5O98 · Alcohol dehydrogenase 1: “Binary complex of catharanthus roseus vitrosamine synthase with NADP+”. X-ray diffraction, 1 ligand (NAP), 2 pockets (best druggability 0.87). MolNFT v1 #129061 on GenesisL1: 3D structure, binding sites and…

PDB: 5O98
Type: protein
Length: 565 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alcohol dehydrogenase 1
UniProt: A0A0C5DR25
Ligands: NAP
Pockets: 2 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alcohol dehydrogenase 1	protein	282	47% helix, 15% strand	A0A0C5DR25
B	Alcohol dehydrogenase 1	protein	283	47% helix, 15% strand	A0A0C5DR25

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B

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	1112	0.87	0.88	115	NAP
2	105	0.39	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 1153 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5O98 · Binary complex of Catharanthus roseus Vitrosamine Synthase with NADP+ · the same entry in another collection · 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 A0A0C5DR25
Elsewhere: RCSB PDB 5O98 · PDBe 5O98 · UniProt A0A0C5DR25

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