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4XSD

Complex structure of thymidylate synthase from varicella zoster virus with a dUMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004799molecular_functionthymidylate synthase activity
A0005829cellular_componentcytosol
A0006231biological_processdTMP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0032259biological_processmethylation
B0004799molecular_functionthymidylate synthase activity
B0005829cellular_componentcytosol
B0006231biological_processdTMP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0032259biological_processmethylation
C0004799molecular_functionthymidylate synthase activity
C0005829cellular_componentcytosol
C0006231biological_processdTMP biosynthetic process
C0006235biological_processdTTP biosynthetic process
C0008168molecular_functionmethyltransferase activity
C0009165biological_processnucleotide biosynthetic process
C0016741molecular_functiontransferase activity, transferring one-carbon groups
C0032259biological_processmethylation
D0004799molecular_functionthymidylate synthase activity
D0005829cellular_componentcytosol
D0006231biological_processdTMP biosynthetic process
D0006235biological_processdTTP biosynthetic process
D0008168molecular_functionmethyltransferase activity
D0009165biological_processnucleotide biosynthetic process
D0016741molecular_functiontransferase activity, transferring one-carbon groups
D0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue UMP A 1001
ChainResidue
AARG38
AASN214
AHIS244
ATYR246
BARG163
BARG164
ACYS183
AHIS184
AGLN202
AARG203
ASER204
AGLY205
AASP206
AGLY210

site_idAC2
Number of Residues11
Detailsbinding site for residue UMP B 1001
ChainResidue
AARG163
AARG164
BCYS183
BGLN202
BARG203
BGLY205
BASP206
BASN214
BHIS244
BTYR246
BHOH1101

site_idAC3
Number of Residues11
Detailsbinding site for residue UMP C 1001
ChainResidue
CARG38
CCYS183
CARG203
CGLY205
CASP206
CGLY210
CVAL211
CASN214
CTYR246
DARG163
DARG164

site_idAC4
Number of Residues12
Detailsbinding site for residue UMP D 1001
ChainResidue
CARG163
CARG164
DCYS183
DHIS184
DGLN202
DARG203
DSER204
DGLY205
DASP206
DASN214
DHIS244
DTYR246

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrmIissWNpkdiplmv.....LpPCHtlcQFyV
ChainResidueDetails
AARG163-VAL191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
ACYS183
BCYS183
CCYS183
DCYS183

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
AARG38
CARG203
CASN214
CHIS244
DARG38
DARG203
DASN214
DHIS244
AARG203
AASN214
AHIS244
BARG38
BARG203
BASN214
BHIS244
CARG38

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
AARG163
AASP206
BARG163
BASP206
CARG163
CASP206
DARG163
DASP206

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PDB entries from 2024-07-10

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