PDBsum entry 3nxo

Oxidoreductase

PDB id: 3nxo

Contents

Protein chain

186 a.a. *

Ligands

D2B

SO4 ×5

NDP

Waters ×165

* Residue conservation analysis

PDB id:

3nxo

Name:

Oxidoreductase

Title:

Perferential selection of isomer binding from chiral mixtures: alternate binding modes observed for the e- and z-isomers of a series of 5-substituted 2,4-diaminofuro[2,3-d]pyrimidines as ternary complexes with NADPH and human dihydrofolate reductase

Structure:

Dihydrofolate reductase. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dhfr, dhfrp1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.35Å R-factor: 0.192 R-free: 0.209

Authors:

V.Cody

Key ref:

V.Cody et al. (2010). Preferential selection of isomer binding from chiral mixtures: alternate binding modes observed for the E and Z isomers of a series of 5-substituted 2,4-diaminofuro[2,3-d]pyrimidines as ternary complexes with NADPH and human dihydrofolate reductase. Acta Crystallogr D Biol Crystallogr, 66, 1271-1277. PubMed id: 21123866

Date:

14-Jul-10 Release date: 01-Dec-10

Protein chain

P00374  (DYR_HUMAN) -  Dihydrofolate reductase from Homo sapiens

Seq: 187 a.a.

Struc: 186 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.1.5.1.3 - dihydrofolate reductase.
• Pathway: Folate Coenzymes
• Reaction: (6S)-5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH + H⁺

(6S)-5,6,7,8-tetrahydrofolate + NADP(+) (Bound ligand (Het Group name = NDP) corresponds exactly) = 7,8-dihydrofolate + NADPH + H(+)

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

reference

Acta Crystallogr D Biol Crystallogr 66:1271-1277 (2010)

PubMed id: 21123866

Preferential selection of isomer binding from chiral mixtures: alternate binding modes observed for the E and Z isomers of a series of 5-substituted 2,4-diaminofuro[2,3-d]pyrimidines as ternary complexes with NADPH and human dihydrofolate reductase.

V.Cody, J.Piraino, J.Pace, W.Li, A.Gangjee.

ABSTRACT

No abstract given.