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2FZH

New Insights into Dihydrofolate Reductase Interactions: Analysis of Pneumocystis carinii and Mouse DHFR Complexes with NADPH and Two Highly Potent Trimethoprim Derivatives

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NDP A 207
ChainResidue
AVAL11
AARG59
ALYS60
ATHR61
AILE80
ATHR81
AARG82
AASN83
ALYS96
AILE123
AGLY124
AALA12
AGLY125
AALA126
AGLN127
ALEU128
ATYR129
AALA131
ADH1208
AHOH215
AHOH216
AHOH247
AILE19
AHOH266
AGLY20
AARG21
ASER24
ALEU25
ATRP27
AGLY58

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE DH1 A 208
ChainResidue
AILE10
AVAL11
AALA12
ALEU25
AGLU32
AILE33
APHE36
ALYS37
APHE69
ALEU72
AARG75
AILE123
ATYR129
ATHR144
ANDP207
AHOH215
AHOH231

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGrsnsLPWklkk.EisyFkrvT
ChainResidueDetails
AGLY18-THR40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10194348, ECO:0000269|PubMed:10736154, ECO:0000269|PubMed:12037296, ECO:0000269|PubMed:12198294, ECO:0000269|PubMed:17019704
ChainResidueDetails
AGLY124
AALA12
AGLY18
AARG59
ATHR81

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:10194348
ChainResidueDetails
AARG75
AGLU32

221051

PDB entries from 2024-06-12

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