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4O1U

Crystal structure of human thymidylate synthase mutant Y202C

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0004799molecular_functionthymidylate synthase activity
A0005542molecular_functionfolic acid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006231biological_processdTMP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0016020cellular_componentmembrane
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
B0005542molecular_functionfolic acid binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006231biological_processdTMP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0016020cellular_componentmembrane
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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AARG78
AARG185
ALEU189
APRO305
ATHR306
BARG176
BHOH559

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AHIS196
AARG215
ASER216
AHOH552
BARG175
AARG50
AASN183

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
AGLN36
AGLN62
AALA63
AVAL223
AHIS250
ALEU252
AHOH590

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
AASP218
AHOH555

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 406
ChainResidue
AARG274
AHIS304
AHOH551

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
AARG176
BARG78
BARG185
BLEU189
BPRO305
BTHR306

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 402
ChainResidue
BARG274
BHIS304
BHOH570

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
AARG175
BASN183
BHIS196
BARG215
BSER216

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 404
ChainResidue
BGLN36
BGLN62
BALA63
BVAL223
BHIS250
BHOH588

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 405
ChainResidue
BPHE142

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 406
ChainResidue
BASP218

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplma.....LpPCHalcQFcV
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 Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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