PDBsum entry 3o2n

Oxidoreductase

PDB id: 3o2n

Contents

Protein chain

230 a.a.

Ligands

FAD ×2

MZX ×3

Metals

_ZN ×2

Waters ×396

PDB id:

3o2n

Name:

Oxidoreductase

Title:

X-ray crystallographic structure activity relationship (sar) of casimiroin and its analogs bound to human quinone reductase 2

Structure:

Ribosyldihydronicotinamide dehydrogenase [quinone]. Chain: a, b. Synonym: nrh dehydrogenase [quinone] 2, nrh:quinone oxidoreductase 2, quinone reductase 2, qr2. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: nqo2, nmor2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å R-factor: 0.184 R-free: 0.220

Authors:

M.Sturdy

Key ref:

M.Sturdy X-Ray crystallographic structure activity relationshi of casimiroin and its analogs bound to human quinone reductase 2. To be published, .

Date:

22-Jul-10 Release date: 03-Aug-11

Protein chains

P16083  (NQO2_HUMAN) -  Ribosyldihydronicotinamide dehydrogenase [quinone] from Homo sapiens

Seq: 231 a.a.

Struc: 230 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.1.10.5.1 - ribosyldihydronicotinamide dehydrogenase (quinone).
• Reaction: 1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone + H⁺ = beta-nicotinamide D-riboside + a quinol

1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide (Bound ligand (Het Group name = MZX) matches with 54.55% similarity) + quinone + H(+) = beta-nicotinamide D-riboside + quinol

• Cofactor: FAD; Zn(2+)

FAD (Bound ligand (Het Group name = FAD) corresponds exactly) Zn(2+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site