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3CD2

LIGAND INDUCED CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURES OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE COMPLEXES WITH FOLATE AND NADP+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
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 Residues23
DetailsBINDING SITE FOR RESIDUE NAP A 207
ChainResidue
AALA12
AILE19
AGLY20
AARG21
ASER24
ALEU25
AGLY58
AARG59
ALYS60
ATHR61
AILE80
ATHR81
AARG82
AASN83
ALYS96
AILE123
AGLY125
AALA126
AGLN127
ALEU128
ATYR129
AHOH252
AMTX307

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MTX A 307
ChainResidue
AILE10
AVAL11
ALEU25
AGLU32
AILE33
APHE36
APHE69
AARG75
AILE123
ATYR129
ANAP207
AHOH252

site_idS1
Number of Residues11
DetailsTHE BINDING ORIENTATION OF THE PTERIDINE RING OF FA IN THIS STRUCTURE IS SIMILAR TO THAT OBSERVED IN HDHFR FA BINARY COMPLEXES.
ChainResidue
AILE10
ATYR129
ATHR144
ALEU25
ATRP27
AGLU32
AILE33
APHE36
AILE65
APRO66
AILE123

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
AALA12
AGLY18
AARG59
ATHR81
AGLY124

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

218853

PDB entries from 2024-04-24

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