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1QQQ

CRYSTAL STRUCTURE ANALYSIS OF SER254 MUTANT OF ESCHERICHIA COLI THYMIDYLATE SYNTHASE

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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 320
ChainResidue
AARG225
AHIS255
AHOH410

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 321
ChainResidue
AHOH539
AARG21
AARG126
AARG127
AARG166
AHOH373
AHOH536

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 322
ChainResidue
AHIS51
AARG53
ASER54
AHOH394
AHOH397
AHOH398
AHOH492

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 Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008, ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0000269|PubMed:9416600
ChainResidueDetails
ACME146

site_idSWS_FT_FI2
Number of Residues4
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

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:8312270, ECO:0007744|PDB:1TYS
ChainResidueDetails
AHIS51
AASP169
AALA263

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC
ChainResidueDetails
AARG126

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1lcb
ChainResidueDetails
AHIS207
AGLU58
AASP169
ASER167
ACME146
AASP205

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PDB entries from 2024-09-04

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