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4PSY

100K crystal structure of Escherichia coli dihydrofolate reductase

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 Residues25
DetailsBINDING SITE FOR RESIDUE FOL A 201
ChainResidue
AILE5
AILE50
AARG57
AILE94
ATHR113
ANAP202
AHOH307
AHOH326
AHOH335
AHOH351
AHOH428
AALA6
AHOH469
AHOH470
AHOH481
AHOH522
AHOH591
AHOH593
AALA7
AMET20
AASP27
ALEU28
AALA29
APHE31
ALYS32

site_idAC2
Number of Residues39
DetailsBINDING SITE FOR RESIDUE NAP A 202
ChainResidue
AALA6
AALA7
AILE14
AGLY15
AASN18
AALA19
AMET20
ATRP22
AGLY43
AARG44
AHIS45
ATHR46
ASER49
ALEU62
ASER63
ASER64
AGLN65
ALYS76
AILE94
AGLY96
AGLY97
AARG98
AVAL99
ATYR100
AGLN102
ATHR123
AASP131
AFOL201
AHOH314
AHOH334
AHOH339
AHOH347
AHOH351
AHOH357
AHOH385
AHOH508
AHOH537
AHOH548
AHOH587

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 203
ChainResidue
AASP116
AHIS149
AARG159
AHOH568
AHOH569
AHOH583

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 204
ChainResidue
AGLU154
AHOH562
AHOH563
AHOH564
AHOH565
AHOH566

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

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PDB entries from 2024-07-31

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