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5NOO

Crystal Structure of C.elegans Thymidylate Synthase in Complex with dUMP and Tomudex

Replaces:  4IQQ
Functional Information from GO Data
ChainGOidnamespacecontents
A0004799molecular_functionthymidylate synthase activity
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
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
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
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 Residues13
Detailsbinding site for residue UMP A 401
ChainResidue
AARG51
ATYR260
AD16402
BARG177
BARG178
ACYS197
AGLN216
AARG217
ASER218
AASP220
AGLY224
AASN228
AHIS258

site_idAC2
Number of Residues8
Detailsbinding site for residue D16 A 402
ChainResidue
ATYR82
AILE110
AASP220
ALEU223
AGLY224
APHE227
ATYR260
AUMP401

site_idAC3
Number of Residues13
Detailsbinding site for residue UMP B 401
ChainResidue
AARG177
BARG51
BCYS197
BHIS198
BGLN216
BARG217
BSER218
BASP220
BGLY224
BASN228
BHIS258
BTYR260
BD16402

site_idAC4
Number of Residues8
Detailsbinding site for residue D16 B 402
ChainResidue
BTYR82
BILE110
BASP220
BLEU223
BGLY224
BPHE227
BTYR260
BUMP401

site_idAC5
Number of Residues12
Detailsbinding site for residue UMP C 401
ChainResidue
CCYS197
CGLN216
CARG217
CSER218
CGLY219
CASP220
CGLY224
CASN228
CHIS258
CTYR260
CD16402
DARG177

site_idAC6
Number of Residues9
Detailsbinding site for residue D16 C 402
ChainResidue
CARG80
CTYR82
CASP220
CLEU223
CGLY224
CPHE227
CTYR260
CUMP401
CHOH505

site_idAC7
Number of Residues14
Detailsbinding site for residue UMP D 401
ChainResidue
CARG177
CARG178
DCYS197
DHIS198
DGLN216
DARG217
DSER218
DGLY219
DASP220
DGLY224
DASN228
DHIS258
DTYR260
DD16402

site_idAC8
Number of Residues10
Detailsbinding site for residue D16 D 402
ChainResidue
DARG80
DVAL81
DTYR82
DILE110
DASP220
DLEU223
DGLY224
DPHE227
DTYR260
DUMP401

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImsaWNpsdlgqmv.....LpPCHtmcQFyV
ChainResidueDetails
AARG177-VAL205

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PDB entries from 2024-07-24

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