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4RGC

277K Crystal structure of Escherichia Coli dihydrofolate reductase

Replaces:  4PSZ
Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0046654biological_processtetrahydrofolate biosynthetic process
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FOL A 201
ChainResidue
AILE5
AARG57
AILE94
ATHR113
ANAP202
AHOH301
AHOH308
AHOH342
AHOH373
AHOH392
AHOH488
AALA6
AHOH495
AALA7
AMET20
AASP27
ALEU28
APHE31
ALYS32
AILE50

site_idAC2
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAP A 202
ChainResidue
AALA6
AALA7
AILE14
AGLY15
AASN18
AALA19
AMET20
AGLY43
AARG44
AHIS45
ATHR46
ASER49
ALEU62
ASER63
ASER64
ALYS76
AILE94
AGLY96
AGLY97
AARG98
AVAL99
ATYR100
AGLN102
AASP131
AFOL201
AHOH302
AHOH312
AHOH337
AHOH373
AHOH378
AHOH383
AHOH419
AHOH444
AHOH460
AHOH496

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 203
ChainResidue
AASP116
AHIS149
AARG159
AHOH396
AHOH458
AHOH462

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 204
ChainResidue
AGLU154
AHOH459
AHOH461

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

250059

PDB entries from 2026-03-04

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