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3EGY

Crystal Structure of Human Thymidyalte Synthase A191K with Loop 181-197 stabilized in the inactive conformation

Functional Information from GO Data
ChainGOidnamespacecontents
X0000900molecular_functionmRNA regulatory element binding translation repressor activity
X0003729molecular_functionmRNA binding
X0004146molecular_functiondihydrofolate reductase activity
X0004799molecular_functionthymidylate synthase activity
X0005542molecular_functionfolic acid binding
X0005634cellular_componentnucleus
X0005737cellular_componentcytoplasm
X0005739cellular_componentmitochondrion
X0005743cellular_componentmitochondrial inner membrane
X0005759cellular_componentmitochondrial matrix
X0005829cellular_componentcytosol
X0006206biological_processpyrimidine nucleobase metabolic process
X0006231biological_processdTMP biosynthetic process
X0006235biological_processdTTP biosynthetic process
X0006417biological_processregulation of translation
X0007623biological_processcircadian rhythm
X0008168molecular_functionmethyltransferase activity
X0009165biological_processnucleotide biosynthetic process
X0009410biological_processresponse to xenobiotic stimulus
X0009636biological_processresponse to toxic substance
X0014070biological_processresponse to organic cyclic compound
X0016020cellular_componentmembrane
X0016740molecular_functiontransferase activity
X0016741molecular_functiontransferase activity, transferring one-carbon groups
X0017148biological_processnegative regulation of translation
X0019860biological_processuracil metabolic process
X0032259biological_processmethylation
X0032570biological_processresponse to progesterone
X0033189biological_processresponse to vitamin A
X0034097biological_processresponse to cytokine
X0035999biological_processtetrahydrofolate interconversion
X0042803molecular_functionprotein homodimerization activity
X0045471biological_processresponse to ethanol
X0046653biological_processtetrahydrofolate metabolic process
X0046683biological_processresponse to organophosphorus
X0048589biological_processdevelopmental growth
X0051216biological_processcartilage development
X0051384biological_processresponse to glucocorticoid
X0051593biological_processresponse to folic acid
X0060574biological_processintestinal epithelial cell maturation
X0071897biological_processDNA biosynthetic process
X0097421biological_processliver regeneration
X1901363molecular_functionheterocyclic compound binding
X1990825molecular_functionsequence-specific mRNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 416
ChainResidue
XARG78
XARG176
XARG185
XLEU189
XPRO305
XTHR306

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 X 417
ChainResidue
XARG215
XSER216
XARG175
XASN183
XHIS196

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO X 314
ChainResidue
XGLN36
XGLN62
XALA63
XVAL223
XHIS250
XLEU252
XHOH528

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
XCME195

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
XCME195
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

218853

PDB entries from 2024-04-24

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