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4EZ8

Crystal structure of mouse thymidylate sythase in ternary complex with N(4)-hydroxy-2'-deoxycytidine-5'-monophosphate and the cofactor product, dihydrofolate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0003729molecular_functionmRNA binding
A0004146molecular_functiondihydrofolate reductase activity
A0004799molecular_functionthymidylate synthase activity
A0005542molecular_functionfolic acid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006206biological_processpyrimidine nucleobase metabolic process
A0006231biological_processdTMP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0006417biological_processregulation of translation
A0007623biological_processcircadian rhythm
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0014070biological_processresponse to organic cyclic compound
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0017148biological_processnegative regulation of translation
A0019860biological_processuracil metabolic process
A0032259biological_processmethylation
A0032570biological_processresponse to progesterone
A0033189biological_processresponse to vitamin A
A0034097biological_processresponse to cytokine
A0035999biological_processtetrahydrofolate interconversion
A0042803molecular_functionprotein homodimerization activity
A0045471biological_processresponse to ethanol
A0046653biological_processtetrahydrofolate metabolic process
A0046683biological_processresponse to organophosphorus
A0048589biological_processdevelopmental growth
A0051216biological_processcartilage development
A0051384biological_processresponse to glucocorticoid
A0051593biological_processresponse to folic acid
A0060574biological_processintestinal epithelial cell maturation
A0097421biological_processliver regeneration
A1901363molecular_functionheterocyclic compound binding
A1990825molecular_functionsequence-specific mRNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NOH A 401
ChainResidue
AARG44
ASER210
AGLY211
AASP212
AASN220
AHIS250
ATYR252
ADHF402
AHOH510
AHOH534
AHOH564
ATRP103
AHOH692
AARG169
AARG170
ALEU186
ACYS189
AHIS190
AGLN208
AARG209

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE DHF A 402
ChainResidue
APHE74
AILE102
ATRP103
AASN106
AASP212
ALEU215
AGLY216
AMET305
AALA306
ANOH401
AHOH515
AHOH540
AHOH559
AHOH564
AHOH609
AHOH633
AHOH652
AHOH692
AHOH838
AHOH898
AHOH936
AHOH957
AHOH958

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
ALYS41
AGLU42
AASP167
AVAL198
AASN199
AHOH525
AHOH636
AHOH721
AHOH978

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
ATYR295
AHOH539
AHOH614
AHOH695
AHOH850

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNpkdlplma.....LpPCHalcQFyV
ChainResidueDetails
AARG169-VAL197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
ACYS189

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
AARG44
AASN220

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P45352
ChainResidueDetails
AARG169

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P45352
ChainResidueDetails
ACYS189
AARG209
AHIS250

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A884
ChainResidueDetails
AASP212
AALA306

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04818
ChainResidueDetails
ASER108

site_idSWS_FT_FI7
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P04818
ChainResidueDetails
ALYS286
ALYS302

218853

PDB entries from 2024-04-24

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