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3H6D

Structure of the mycobacterium tuberculosis DUTPase D28N 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 Residues1
DetailsBINDING SITE FOR RESIDUE MG A 200
ChainResidue
ADUP201

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE DUP A 201
ChainResidue
ATYR86
AGLU89
AILE90
ALYS91
AGLN113
AARG140
AHOH188
AMG200
AHOH212
AHOH219
AARG64
AHOH222
AHOH245
ASER65
AGLY66
AASN77
AGLY80
ATHR81
AILE82
AASP83

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TRS A 202
ChainResidue
ASER74
ASER74
ASER74
AILE75
AILE75
AILE75
AVAL76
AVAL76
AVAL76
ALEU97
AHOH194
AHOH194
AHOH194

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS A 203
ChainResidue
AARG9
AARG9
AARG9
APRO12
APRO12
APRO12
AHOH208
AHOH208
AHOH208

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

246031

PDB entries from 2025-12-10

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