PDBsum entry 3hq4

Oxidoreductase

PDB id: 3hq4

Contents

Protein chains

334 a.a. *

Ligands

NAD ×4

Waters ×392

* Residue conservation analysis

PDB id:

3hq4

Name:

Oxidoreductase

Title:

Crystal structure of c151s mutant of glyceraldehyde-3-phosphate dehydrogenase 1 (gapdh1) complexed with NAD from staphylococcus aureus mrsa252 at 2.2 angstrom resolution

Structure:

Glyceraldehyde-3-phosphate dehydrogenase 1. Chain: r, o, p, q. Synonym: gapdh 1. Engineered: yes. Mutation: yes

Source:

Staphylococcus aureus subsp. Aureus. Organism_taxid: 282458. Strain: mrsa252. Gene: gap, gap1, gapa, gapa1, sar0828. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.187 R-free: 0.244

Authors:

S.Mukherjee,D.Dutta,B.Saha,A.K.Das

Key ref:

S.Mukherjee et al. (2010). Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus MRSA252 provides novel insights into substrate binding and catalytic mechanism. J Mol Biol, 401, 949-968. PubMed id: 20620151

Date:

05-Jun-09 Release date: 23-Jun-10

Protein chains

Q6GIL8  (G3P1_STAAR) -  Glyceraldehyde-3-phosphate dehydrogenase 1 from Staphylococcus aureus (strain MRSA252)

Seq: 336 a.a.

Struc: 334 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating).
• Pathway: Glyceraldehyde-3-phosphate Dehydrogenase (phosphorylating)
• Reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD⁺ = (2R)-3-phospho- glyceroyl phosphate + NADH + H⁺

D-glyceraldehyde 3-phosphate + phosphate (Bound ligand (Het Group name = NAD) corresponds exactly) + NAD(+) = (2R)-3-phospho- glyceroyl phosphate + NADH + H(+)

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

reference

J Mol Biol 401:949-968 (2010)

PubMed id: 20620151

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus MRSA252 provides novel insights into substrate binding and catalytic mechanism.

S.Mukherjee, D.Dutta, B.Saha, A.K.Das.

ABSTRACT

No abstract given.