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2QLP

Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0006229biological_processdUTP biosynthetic process
A0008829molecular_functiondCTP deaminase activity
B0006229biological_processdUTP biosynthetic process
B0008829molecular_functiondCTP deaminase activity
C0006229biological_processdUTP biosynthetic process
C0008829molecular_functiondCTP deaminase activity
D0006229biological_processdUTP biosynthetic process
D0008829molecular_functiondCTP deaminase activity
E0006229biological_processdUTP biosynthetic process
E0008829molecular_functiondCTP deaminase activity
F0006229biological_processdUTP biosynthetic process
F0008829molecular_functiondCTP deaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE A 162
ChainResidue
AARG106
ALEU107
CARG41
CLEU81
CSER83

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE 1PE A 163
ChainResidue
AARG41

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE B 162
ChainResidue
CARG106
BARG41
BSER83
BTHR127

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE C 162
ChainResidue
CGLN65
CVAL67
CASP68

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE D 162
ChainResidue
DARG41
DGLY82
DSER83
EARG106

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE E 162
ChainResidue
EARG41
ELEU81
EGLY82
ETHR127

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE F 162
ChainResidue
DARG106
FARG41
FSER83

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P28248","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Dttp inhibition of the bifunctional Dctp deaminase- dutpase from Mycobacterium tuberculosis is pH dependent: kinetic analyses and crystal structure of A115V Variant.","authors":["Lovgreen M.N.","Harris P.","Ucar E.","Willemoes M."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18164314","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Dttp inhibition of the bifunctional Dctp deaminase- dutpase from Mycobacterium tuberculosis is pH dependent: kinetic analyses and crystal structure of A115V Variant.","authors":["Lovgreen M.N.","Harris P.","Ucar E.","Willemoes M."]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Important for bifunctional activity","evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18164314","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
AGLY121
AASP119

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
BGLY121
BASP119

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
CGLY121
CASP119

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
DGLY121
DASP119

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
EGLY121
EASP119

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
FGLY121
FASP119

239803

PDB entries from 2025-08-06

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