PDBsum entry 3rhm

Oxidoreductase

PDB id: 3rhm

Contents

Protein chains

498 a.a.

Ligands

SO4 ×28

GOL ×4

Waters ×683

PDB id:

3rhm

Name:

Oxidoreductase

Title:

Crystal structure of the e673q mutant of c-terminal domain of 10'formyltetrahydrofolate dehydrogenase

Structure:

Aldehyde dehydrogenase 1 family, member l1. Chain: a, b, c, d. Fragment: c-terminal domain, residues 397-902. Engineered: yes. Mutation: yes

Source:

Rattus norvegicus. Brown rat,rat,rats. Organism_taxid: 10116. Gene: aldh1l1, fthfd. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.38Å R-factor: 0.173 R-free: 0.202

Authors:

Y.Tsybovsky

Key ref:

Y.Tsybovsky and S.A.Krupenko (2011). Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain control binding and discharging of the coenzyme. J Biol Chem, 286, 23357-23367. PubMed id: 21540484

Date:

11-Apr-11 Release date: 27-Apr-11

Protein chains

P28037  (AL1L1_RAT) -  Cytosolic 10-formyltetrahydrofolate dehydrogenase from Rattus norvegicus

Seq: 902 a.a.

Struc: 498 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.1.5.1.6 - formyltetrahydrofolate dehydrogenase.
• Pathway: Folate Coenzymes
• Reaction: (6R)-10-formyltetrahydrofolate + NADP⁺ + H2O = (6S)-5,6,7,8- tetrahydrofolate + CO2 + NADPH + H⁺

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

reference

J Biol Chem 286:23357-23367 (2011)

PubMed id: 21540484

Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain control binding and discharging of the coenzyme.

Y.Tsybovsky, S.A.Krupenko.

ABSTRACT

No abstract given.