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1EUW

ATOMIC RESOLUTION STRUCTURE OF E. COLI DUTPASE

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 Residues6
DetailsBINDING SITE FOR RESIDUE EMC A 153
ChainResidue
AASP11
AARG13
ACYS36
ALEU37
AGLY54
AHOH470

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 154
ChainResidue
AGOL155
AHOH266
AHOH401
AHOH424
ASER72
AHIS76
AMET98

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 155
ChainResidue
AILE89
ATYR93
AGLN96
AMET98
AGOL154
AHOH260
AHOH277
AHOH320
AHOH368

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15208312","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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
ASER28activator
APRO70electrostatic stabiliser
ASER72electrostatic stabiliser
AGLY79modifies pKa
AILE89proton acceptor, proton donor

239149

PDB entries from 2025-07-23

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