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1B02

CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS

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
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE UFP A 280
ChainResidue
AARG28
AHIS222
ATYR224
AC2F281
AHOH291
AHOH313
ATYR108
ACYS161
AARG181
ASER182
AASN183
AASP184
AGLY188
AASN192

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE C2F A 281
ChainResidue
AALA64
ATHR67
AILE93
ATRP94
ATRP97
AASP184
AGLY188
AALA278
AUFP280
AHOH299
AHOH332
AHOH342
AHOH351
AHOH360

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrhItmlWNpdeldama.....LtPCVyetQWyV
ChainResidueDetails
AARG141-VAL169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008
ChainResidueDetails
ACYS161

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00008
ChainResidueDetails
AARG141
AASP184
AALA278

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00008
ChainResidueDetails
AARG181
AASN192
AHIS222

218853

PDB entries from 2024-04-24

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