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3HZA

Crystal structure of dUTPase H145W mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004170molecular_functiondUTP diphosphatase activity
A0006226biological_processdUMP biosynthetic process
A0009117biological_processnucleotide metabolic process
A0016787molecular_functionhydrolase activity
A0046080biological_processdUTP metabolic process
A0046081biological_processdUTP catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 200
ChainResidue
ADUP201
AHOH313
AHOH316
AHOH317

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE DUP A 201
ChainResidue
ATHR81
AILE82
AASP83
ATYR86
AILE90
ALYS91
AGLN113
AARG140
AGLY144
ATRP145
AGLY146
ASER147
ASER148
AMG200
AHOH302
AHOH303
AHOH305
AHOH313
AHOH316
AHOH317
AHOH324
AARG64
ASER65
AGLY66
AASN77
AGLY80

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
AALA6
AALA100
AALA101
APRO102
AALA133
ALEU135
AHOH386

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 203
ChainResidue
AASP131
AHOH347
AHOH442

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 204
ChainResidue
ASER74
ASER74
AILE75
AVAL76
AHOH402
AHOH402
AHOH402

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00116","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15276840","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15276840","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
AGLY85
AASP83

247536

PDB entries from 2026-01-14

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