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5H3A

Structural analysis of KSHV thymidylate synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004799molecular_functionthymidylate synthase activity
A0006231biological_processdTMP biosynthetic process
A0016741molecular_functiontransferase activity, transferring one-carbon groups
B0004799molecular_functionthymidylate synthase activity
B0006231biological_processdTMP biosynthetic process
B0016741molecular_functiontransferase activity, transferring one-carbon groups
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue D16 A 401
ChainResidue
APHE104
AASP242
ALEU245
AGLY246
APHE249
AUMP402

site_idAC2
Number of Residues13
Detailsbinding site for residue UMP A 402
ChainResidue
ASER240
AGLY241
AASP242
AGLY246
AASN250
AHIS280
ATYR282
AD16401
BARG199
BARG200
ACYS219
AHIS220
AARG239

site_idAC3
Number of Residues5
Detailsbinding site for residue D16 B 401
ChainResidue
BASP242
BLEU245
BGLY246
BPHE249
BUMP402

site_idAC4
Number of Residues14
Detailsbinding site for residue UMP B 402
ChainResidue
AARG199
AARG200
BCYS219
BHIS220
BGLN238
BARG239
BSER240
BGLY241
BASP242
BGLY246
BASN250
BHIS280
BTYR282
BD16401

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNpadlslma.....LpPCHllcQFyV
ChainResidueDetails
AARG199-VAL227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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