Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1viea_ All beta proteins SH3-like barrel Electron transport accessory proteins R67 dihydrofolate reductase R67 dihydrofolate reductase (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyElectron transport accessory proteins8036825 3000325 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ADHFR_2e1vieA1 A: beta barrelsX: SH3H: SH3T: SH3F: DHFR_2ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.30.30.60 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF06442R67 dihydrofolate reductase (DHFR_2)R67 dihydrofolate reductaseR67 dihydrofolate reductase is a plasmid encoded enzyme that provides resistance to the antibacterial drug trimethoprim. The R67 dihydrofolate reductase does not share significant similarity to the chromosomal encoded dihydrofolate reductase [1].Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
DIHYDROFOLATE REDUCTASE -

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
dihydrofolate reductase (type II)  M-CSA #752

R67-plasmid encoded dihydrofolate reductase (R67-DHFR) from Escherichia coli catalyses the reduction of 7,8-dihydrofolate (DHF) to 5,6,7,8-tetrahydrofolate (THF) in the presence of NADPH. It is one of the smallest enzymes known to self-assemble into an active quaternary structure. The tetramer has an unusual pore, 25 angstroms in length that passes through the middle of the molecule and out the other side. R67-DHFR has 222 symmetry, and has a distinctive 'one site fits both' substrate and cofactor.

Defined by 4 residues: LYS:A-16 [auth A-32]GLN:A-51 [auth A-67]ILE:A-52 [auth A-68]TYR:A-53 [auth A-69]
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