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3NZC

Structural Analysis of Pneumocystis carinii and Human DHFR Complexes with NADPH and a Series of Five Potent 5-(omega-carboxy(alkyloxy)pyrido[2,3-d]pyridine Derivativea

Functional Information from GO Data
ChainGOidnamespacecontents
X0004146molecular_functiondihydrofolate reductase activity
X0005739cellular_componentmitochondrion
X0005829cellular_componentcytosol
X0006730biological_processone-carbon metabolic process
X0016491molecular_functionoxidoreductase activity
X0046452biological_processdihydrofolate metabolic process
X0046654biological_processtetrahydrofolate biosynthetic process
X0046655biological_processfolic acid metabolic process
X0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE D2O X 207
ChainResidue
XILE10
XPHE69
XILE123
XTYR129
XGOL210
XHOH249
XVAL11
XALA12
XLEU25
XGLU32
XILE33
XPHE36
XSER64
XPRO66

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 X 208
ChainResidue
XGLY58
XLYS60
XTHR61
XGLY124
XGLY125
XALA126
XGLN127

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL X 209
ChainResidue
XARG107
XSER166
XTRP169
XLYS170
XLYS171
XHOH227

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL X 210
ChainResidue
XALA12
XILE19
XLEU25
XILE123
XTYR129

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGrsnsLPWklkk.EisyFkrvT
ChainResidueDetails
XGLY18-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
XGLY124
XALA12
XGLY18
XARG59
XTHR81

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:10194348
ChainResidueDetails
XGLU32
XARG75

219869

PDB entries from 2024-05-15

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