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1CD2

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 Residues26
DetailsBINDING SITE FOR RESIDUE NAP A 207
ChainResidue
AVAL11
ALYS60
ATHR61
AILE80
ATHR81
AARG82
AASN83
ALYS96
AILE123
AGLY125
AALA126
AALA12
AGLN127
ALEU128
ATYR129
AALA131
AHOH226
AHOH264
AFOL307
AILE19
AGLY20
AASN23
ASER24
ALEU25
AGLY58
AARG59

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FOL A 307
ChainResidue
AILE10
AGLU32
AILE33
APHE36
ALYS37
APHE69
ALEU72
AARG75
AILE123
ANAP207
AHOH264
AHOH265

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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