Het-PDB Navi2 (PDB: 1RB2)

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Ligands
Code	Name		Style	Show	Link
FOL	Folic acid				PoSSuM
NAP	Nadp nicotinamide-adenine-dinucleotide phosphate				PoSSuM

Non-standard Residues
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Glycosylation
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Download interaction data: 1RB2

Code :

1RB2 PDBj RCSB PDB PDBe

Header :

OXIDOREDUCTASE

Title :

DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)

Release Data :

1997-03-12

Compound :

mol_id	molecule	chains	synonym
1	DIHYDROFOLATE REDUCTASE	A,B	DHFR
	ec: 1.5.1.3

Source :

mol_id	organism_scientific	expression_system
1	Escherichia coli (taxid:562)	Escherichia coli (taxid:562)
	strain: RT500 expression_system_plasmid: PRWA-1

Authors :

Sawaya, M.R., Kraut, J.

Keywords :

OXIDOREDUCTASE, NADP, TRIMETHOPRIM RESISTANCE, METHOTREXATE RESISTANCE, ONE-CARBON METABOLISM

Exp. method :

X-RAY DIFFRACTION ( 2.1 Å )

Citation :

Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence.

Sawaya, M.R.,Kraut, J.
(1997) Biochemistry 36 : 586 - 603

PubMed: 9012674
DOI: 10.1021/bi962337c

Isomorphous Crystal Structures of Escherichia Coli Dihydrofolate Reductase Complexed with Folate, 5-Deazafolate, and 5,10-Dideazatetrahydrofolate: Mechanistic Implications

Reyes, V.M.,Sawaya, M.R.,Brown, K.A. et al.
(1995) Biochemistry 34 : 2710

Crystal Structure of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes and Cooperativity in Binding

Bystroff, C.,Kraut, J.
(1991) Biochemistry 30 : 2227

Crystal Structures of Escherichia Coli Dihydrofolate Reductase: The Nadp+ Holoenzyme and the Folate.Nadp+ Ternary Complex. Substrate Binding and a Model for the Transition State

Bystroff, C.,Oatley, S.J.,Kraut, J.
(1990) Biochemistry 29 : 3263

Chain :

A, B

UniProt :

P0ABQ4 (DYR_ECOLI)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH	1.5.1.3	PROSITE- ProRule:PRU00660, PubMed:16510443
	-	PROSITE- ProRule:PRU00660, PubMed:16510443

PDB ID: 1RB2

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