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1EU5

STRUCTURE OF E. COLI DUTPASE AT 1.45 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004170molecular_functiondUTP diphosphatase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006226biological_processdUMP biosynthetic process
A0009117biological_processnucleotide metabolic process
A0016787molecular_functionhydrolase activity
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046081biological_processdUTP catabolic process
A0046872molecular_functionmetal ion binding
A0070207biological_processprotein homotrimerization
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 153
ChainResidue
ASER72
AHIS76
AMET98
AGOL154
AHOH264
AHOH398
AHOH405

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 154
ChainResidue
AGLN96
AMET98
AGOL153
AHOH260
AHOH274
AHOH317
AHOH405
AHOH406
AILE89
ATYR93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER72

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15208312
ChainResidueDetails
ALEU85
AILE99

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AILE89

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
AASP90
AASP92

site_idMCSA1
Number of Residues5
DetailsM-CSA 844
ChainResidueDetails
AALA29activator
AARG71electrostatic stabiliser
AGLY73electrostatic stabiliser
AILE80modifies pKa
AASP90proton acceptor, proton donor

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PDB entries from 2024-09-18

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