Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5X67

Human thymidylate synthase in complex with dUMP and nolatrexed

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0004799molecular_functionthymidylate synthase activity
A0005515molecular_functionprotein binding
A0005542molecular_functionfolic acid binding
A0005634cellular_componentnucleus
A0005657cellular_componentreplication fork
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006231biological_processdTMP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0006260biological_processDNA replication
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0016740molecular_functiontransferase activity
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0017148biological_processnegative regulation of translation
A0032259biological_processmethylation
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
A0071897biological_processDNA biosynthetic process
A1990825molecular_functionsequence-specific mRNA binding
B0000900molecular_functionmRNA regulatory element binding translation repressor activity
B0004799molecular_functionthymidylate synthase activity
B0005515molecular_functionprotein binding
B0005542molecular_functionfolic acid binding
B0005634cellular_componentnucleus
B0005657cellular_componentreplication fork
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006231biological_processdTMP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0006260biological_processDNA replication
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0016740molecular_functiontransferase activity
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0017148biological_processnegative regulation of translation
B0032259biological_processmethylation
B0035999biological_processtetrahydrofolate interconversion
B0046653biological_processtetrahydrofolate metabolic process
B0071897biological_processDNA biosynthetic process
B1990825molecular_functionsequence-specific mRNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue UMP A 401
ChainResidue
AARG50
ATYR258
A7Z9402
AHOH527
AHOH529
BARG175
BARG176
ACYS195
AHIS196
AGLN214
AARG215
ASER216
AASP218
AASN226
AHIS256

site_idAC2
Number of Residues12
Detailsbinding site for residue 7Z9 A 402
ChainResidue
AILE108
ATRP109
AASN112
AASP218
ALEU221
AGLY222
APHE225
AMET311
AALA312
AUMP401
AHOH531
AHOH555

site_idAC3
Number of Residues16
Detailsbinding site for residue UMP B 401
ChainResidue
AARG175
AARG176
BARG50
BCYS195
BHIS196
BGLN214
BARG215
BSER216
BGLY217
BASP218
BASN226
BHIS256
BTYR258
B7Z9402
BHOH522
BHOH572

site_idAC4
Number of Residues11
Detailsbinding site for residue 7Z9 B 402
ChainResidue
BILE108
BTRP109
BASN112
BASP218
BLEU221
BGLY222
BPHE225
BMET311
BALA312
BUMP401
BHOH518

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplma.....LpPCHalcQFyV
ChainResidueDetails
AARG175-VAL203

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 Residues4
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P45352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P45352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon