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3I3R

X-ray structure dihydrofolate reductase/thymidylate synthase from babesia bovis at 2.35A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004146molecular_functiondihydrofolate reductase activity
A0004799molecular_functionthymidylate synthase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006231biological_processdTMP biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0032259biological_processmethylation
A0046654biological_processtetrahydrofolate biosynthetic process
B0000166molecular_functionnucleotide binding
B0004146molecular_functiondihydrofolate reductase activity
B0004799molecular_functionthymidylate synthase activity
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006231biological_processdTMP biosynthetic process
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0032259biological_processmethylation
B0046654biological_processtetrahydrofolate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
AARG248
AARG413
BARG374

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 601
ChainResidue
BARG248
BARG413

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrlIvcsWNvsdlkkma.....LpPCHcffQFyV
ChainResidueDetails
AARG373-VAL401

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
ACYS393
ASER427
AASN424

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
BCYS393
BSER427
BASN424

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
AASP37
AILE29

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
BASP37
BILE29

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
AASP452
AHIS454
AGLU285
ASER414
AASP416
ACYS393

site_idCSA6
Number of Residues6
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
BASP452
BHIS454
BGLU285
BSER414
BASP416
BCYS393

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PDB entries from 2024-10-09

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