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5DFR

CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL CHANGES AND COOPERATIVITY IN BINDING

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005515molecular_functionprotein binding
A0005542molecular_functionfolic acid binding
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0009410biological_processresponse to xenobiotic stimulus
A0016491molecular_functionoxidoreductase activity
A0031427biological_processresponse to methotrexate
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0046677biological_processresponse to antibiotic
A0050661molecular_functionNADP binding
A0051870molecular_functionmethotrexate binding
A0051871molecular_functiondihydrofolic acid binding
A0070401molecular_functionNADP+ binding
A0070402molecular_functionNADPH binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
ALYS32
AHOH338
AHOH372
ACL503

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 502
ChainResidue
AHIS114

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AHOH338
ACL501

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.DlawFkrnT
ChainResidueDetails
AVAL13-THR35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:9012674
ChainResidueDetails
ATHR113
AILE5
AASP27
AARG52
AARG57

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19374017
ChainResidueDetails
AVAL13
AHIS45
ASER63
ALYS76
AGLY95
AALA7

218500

PDB entries from 2024-04-17

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