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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4FOG

Crystal Structure of Mtb ThyA in Complex with 5-Fluoro-dUMP and 5-methyltetrahydrofolic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004799molecular_functionthymidylate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006231biological_processdTMP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0016740molecular_functiontransferase activity
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0032259biological_processmethylation
A0046079biological_processdUMP catabolic process
A0046677biological_processresponse to antibiotic
B0004799molecular_functionthymidylate synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006231biological_processdTMP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0016740molecular_functiontransferase activity
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0032259biological_processmethylation
B0046079biological_processdUMP catabolic process
B0046677biological_processresponse to antibiotic
C0004799molecular_functionthymidylate synthase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006231biological_processdTMP biosynthetic process
C0006235biological_processdTTP biosynthetic process
C0008168molecular_functionmethyltransferase activity
C0009165biological_processnucleotide biosynthetic process
C0016740molecular_functiontransferase activity
C0016741molecular_functiontransferase activity, transferring one-carbon groups
C0032259biological_processmethylation
C0046079biological_processdUMP catabolic process
C0046677biological_processresponse to antibiotic
D0004799molecular_functionthymidylate synthase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006231biological_processdTMP biosynthetic process
D0006235biological_processdTTP biosynthetic process
D0008168molecular_functionmethyltransferase activity
D0009165biological_processnucleotide biosynthetic process
D0016740molecular_functiontransferase activity
D0016741molecular_functiontransferase activity, transferring one-carbon groups
D0032259biological_processmethylation
D0046079biological_processdUMP catabolic process
D0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE UFP A 301
ChainResidue
ATYR94
ATYR209
AC2F302
AHOH420
DARG126
DARG127
ACYS146
AHIS147
AGLN165
AARG166
ASER167
AASP169
AASN177
AHIS207
site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE C2F A 302
ChainResidue
AHIS51
ASER54
AILE79
ATRP83
ALEU143
AASP169
AGLY173
APHE176
ATYR209
AUFP301
site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UFP B 301
ChainResidue
BTYR94
BCYS146
BHIS147
BGLN165
BARG166
BSER167
BALA168
BASP169
BGLY173
BASN177
BHIS207
BTYR209
BHOH439
BHOH440
CARG126
site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UFP C 301
ChainResidue
BARG126
BARG127
CARG21
CTYR94
CCYS146
CHIS147
CGLN165
CARG166
CSER167
CASP169
CASN177
CHIS207
CTYR209
CC2F302
CHOH416
site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE C2F C 302
ChainResidue
CHIS51
CSER54
CILE79
CTRP83
CLEU143
CASP169
CGLY173
CPHE176
CVAL261
CALA262
CUFP301
CHOH452
CHOH456
CHOH459
site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE UFP D 301
ChainResidue
AARG126
AARG127
AHOH440
DARG21
DTYR94
DCYS146
DHIS147
DGLN165
DARG166
DSER167
DALA168
DASP169
DASN177
DHIS207
DTYR209
DC2F302
DHOH484
site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE C2F D 302
ChainResidue
DILE79
DTRP80
DTRP83
DLEU143
DASP169
DLEU172
DGLY173
DILE257
DALA262
DUFP301
DHOH425
DHOH467
DHOH477
DHOH484
Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriIvsaWNvgeierma.....LpPCHaffQFyV
ChainResidueDetails
AARG126-VAL154
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00008","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues27
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"3QJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FOX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FQS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"4FOG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"3QJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FOX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FQS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

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