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3I93

Crystal structure of Mycobacterium tuberculosis dUTPase STOP138T mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004170molecular_functiondUTP diphosphatase activity
A0006220biological_processpyrimidine nucleotide metabolic process
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
AHOH383
AHOH384
AHOH395

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE DUP A 201
ChainResidue
ATHR81
AILE82
AASP83
ATYR86
AGLU89
AILE90
ALYS91
AGLN113
AMG200
AHOH323
AHOH324
AHOH353
AHOH355
AHOH383
AHOH384
AHOH395
AARG64
ASER65
AGLY66
AASN77
AGLY80

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TRS A 202
ChainResidue
ASER74
ASER74
AILE75
AVAL76
AHOH309
AHOH309

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 203
ChainResidue
AARG9
AARG9
APRO12
APRO12
APRO12
AHOH356
AHOH389
AHOH389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00116, ECO:0000269|PubMed:15276840
ChainResidueDetails
AARG64
AASN77
ATHR81

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15276840
ChainResidueDetails
ALYS91

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

222036

PDB entries from 2024-07-03

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