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3KGB

Crystal structure of thymidylate synthase 1/2 from Encephalitozoon cuniculi at 2.2 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004799molecular_functionthymidylate synthase activity
A0005739cellular_componentmitochondrion
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 300
ChainResidue
AGLY199
AVAL236
ATYR237
AHIS240

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriVvsaWNptdlgsma.....LpPCHvlfQFnV
ChainResidueDetails
AARG154-VAL182

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
ACYS174

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
AARG29
AARG194
AASN205
AHIS235

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
AARG154
AASP197

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
ASER208
ACYS174
AASN205

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
ASER195
ACYS174
AASP197
AGLU67
AASP233
AHIS235

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PDB entries from 2024-07-24

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