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3EDW

Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability

Functional Information from GO Data
ChainGOidnamespacecontents
X0000900molecular_functionmRNA regulatory element binding translation repressor activity
X0004799molecular_functionthymidylate synthase activity
X0005542molecular_functionfolic acid binding
X0005634cellular_componentnucleus
X0005737cellular_componentcytoplasm
X0005739cellular_componentmitochondrion
X0005743cellular_componentmitochondrial inner membrane
X0005759cellular_componentmitochondrial matrix
X0005829cellular_componentcytosol
X0006231biological_processdTMP biosynthetic process
X0006235biological_processdTTP biosynthetic process
X0008168molecular_functionmethyltransferase activity
X0009165biological_processnucleotide biosynthetic process
X0016020cellular_componentmembrane
X0016740molecular_functiontransferase activity
X0016741molecular_functiontransferase activity, transferring one-carbon groups
X0017148biological_processnegative regulation of translation
X0032259biological_processmethylation
X0035999biological_processtetrahydrofolate interconversion
X0046653biological_processtetrahydrofolate metabolic process
X0071897biological_processDNA biosynthetic process
X1990825molecular_functionsequence-specific mRNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 X 315
ChainResidue
XGLU272
XARG274
XHIS304
XHOH393

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 317
ChainResidue
XHOH349
XARG175
XASN183
XARG185
XARG215
XSER216

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 X 318
ChainResidue
XARG50
XARG78
XARG176
XARG185
XLEU189
XPRO305
XTHR306

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplma.....LpPCHalcQFyV
ChainResidueDetails
XARG175-VAL203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
XCYS195

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
XARG50
XASN226

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P45352
ChainResidueDetails
XARG175

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P45352
ChainResidueDetails
XCYS195
XARG215
XHIS256

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
XASP218
XALA312

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
XSER114

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
XLYS287
XLYS292
XLYS308

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PDB entries from 2025-07-02

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