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4PST

Multiconformer model for Escherichia coli dihydrofolate reductase at 277 K

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 Residues22
DetailsBINDING SITE FOR RESIDUE FOL A 201
ChainResidue
AILE5
ALEU54
AARG57
AILE94
ATHR113
ANAP202
AHOH301
AHOH308
AHOH342
AHOH373
AHOH392
AALA6
AHOH470
AHOH492
AHOH493
AALA7
AMET20
AASP27
ALEU28
APHE31
ALYS32
AILE50

site_idAC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE NAP A 202
ChainResidue
AALA6
AALA7
AILE14
AGLY15
AASN18
AALA19
AMET20
AGLY43
AARG44
AHIS45
ATHR46
ASER49
ALEU62
ASER63
ASER64
AGLN65
ALYS76
AILE94
AGLY96
AGLY97
AARG98
AVAL99
ATYR100
AGLN102
ATHR123
AASP131
AFOL201
AHOH302
AHOH312
AHOH337
AHOH373
AHOH378
AHOH383
AHOH419
AHOH420
AHOH434
AHOH445
AHOH461

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 203
ChainResidue
AASP116
AHIS149
AARG159
AHOH396
AHOH459
AHOH463

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 204
ChainResidue
AGLU154
AHOH460
AHOH462

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

237735

PDB entries from 2025-06-18

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