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2OIP

Crystal Structure of the S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0004799molecular_functionthymidylate synthase activity
A0006231biological_processdTMP biosynthetic process
A0006730biological_processone-carbon metabolic process
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0046654biological_processtetrahydrofolate biosynthetic process
B0004146molecular_functiondihydrofolate reductase activity
B0004799molecular_functionthymidylate synthase activity
B0006231biological_processdTMP biosynthetic process
B0006730biological_processone-carbon metabolic process
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0046654biological_processtetrahydrofolate biosynthetic process
C0004146molecular_functiondihydrofolate reductase activity
C0004799molecular_functionthymidylate synthase activity
C0006231biological_processdTMP biosynthetic process
C0006730biological_processone-carbon metabolic process
C0016741molecular_functiontransferase activity, transferring one-carbon groups
C0046654biological_processtetrahydrofolate biosynthetic process
D0004146molecular_functiondihydrofolate reductase activity
D0004799molecular_functionthymidylate synthase activity
D0006231biological_processdTMP biosynthetic process
D0006730biological_processone-carbon metabolic process
D0016741molecular_functiontransferase activity, transferring one-carbon groups
D0046654biological_processtetrahydrofolate biosynthetic process
E0004146molecular_functiondihydrofolate reductase activity
E0004799molecular_functionthymidylate synthase activity
E0006231biological_processdTMP biosynthetic process
E0006730biological_processone-carbon metabolic process
E0016741molecular_functiontransferase activity, transferring one-carbon groups
E0046654biological_processtetrahydrofolate biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGingqLPWsise.DlkfFskiT
ChainResidueDetails
AGLY18-THR40

site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrhIltaWNpsalsqma.....LpPCHvlsQYyV
ChainResidueDetails
AARG382-VAL410

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
AASP426
AASP462
AGLU294
AHIS464
ASER424
ACYS402

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
ELEU25
EASP32

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
DASP426
DASP462
DGLU294
DHIS464
DSER424
DCYS402

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
CASP426
CASP462
CGLU294
CHIS464
CSER424
CCYS402

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
EASP426
EASP462
EGLU294
EHIS464
ESER424
ECYS402

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
BASP426
BASP462
BGLU294
BHIS464
BSER424
BCYS402

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
ALEU25
AASP32

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
BLEU25
BASP32

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
CLEU25
CASP32

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
DLEU25
DASP32

223790

PDB entries from 2024-08-14

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