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6CDZ

E. coli thymidylate synthase mutant I264Am

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0004799molecular_functionthymidylate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006231biological_processdTMP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0006417biological_processregulation of translation
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0009314biological_processresponse to radiation
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0032259biological_processmethylation
A0042803molecular_functionprotein homodimerization activity
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0004799molecular_functionthymidylate synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006231biological_processdTMP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0006417biological_processregulation of translation
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0009314biological_processresponse to radiation
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0032259biological_processmethylation
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue CB3 A 701
ChainResidue
AHIS51
AVAL262
AALA263
AUMP702
AHOH816
AHOH829
AHOH835
AHOH843
AASN76
AILE79
AASP169
ALEU172
AGLY173
APHE176
AASN177
ATYR209

site_idAC2
Number of Residues15
Detailsbinding site for residue UMP A 702
ChainResidue
AARG21
ACYS146
AHIS147
AGLN165
AARG166
ASER167
ACYS168
AASP169
AASN177
AHIS207
ATYR209
ACB3701
AHOH807
AHOH862
BARG126

site_idAC3
Number of Residues16
Detailsbinding site for residue CB3 B 301
ChainResidue
BASN76
BILE79
BTRP83
BASP169
BLEU172
BGLY173
BPHE176
BASN177
BTYR209
BALA263
BUMC302
BHOH401
BHOH421
BHOH425
BHOH426
BHOH435

site_idAC4
Number of Residues14
Detailsbinding site for residue UMC B 302
ChainResidue
AARG126
AARG127
BARG21
BCYS146
BHIS147
BGLN165
BARG166
BSER167
BASP169
BASN177
BHIS207
BTYR209
BCB3301
BHOH445

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriIvsaWNvgeldkma.....LaPCHaffQFyV
ChainResidueDetails
AARG126-VAL154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008, ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0000269|PubMed:9416600
ChainResidueDetails
ACYS146
BCYS146

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: in other chain => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC
ChainResidueDetails
AARG21
AARG166
AASN177
AHIS207
BARG21
BARG166
BASN177
BHIS207

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:8312270, ECO:0007744|PDB:1TYS
ChainResidueDetails
AHIS51
AASP169
AALA263
BHIS51
BASP169
BALA263

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC
ChainResidueDetails
AARG126
BARG126

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PDB entries from 2024-07-17

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