Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ZHX

Crystal structure of Uracil-DNA Glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0097510biological_processbase-excision repair, AP site formation via deaminated base removal
B0005515molecular_functionprotein binding
C0004844molecular_functionuracil DNA N-glycosylase activity
C0005737cellular_componentcytoplasm
C0006281biological_processDNA repair
C0006284biological_processbase-excision repair
C0016787molecular_functionhydrolase activity
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0097510biological_processbase-excision repair, AP site formation via deaminated base removal
D0005515molecular_functionprotein binding
E0004844molecular_functionuracil DNA N-glycosylase activity
E0005737cellular_componentcytoplasm
E0006281biological_processDNA repair
E0006284biological_processbase-excision repair
E0016787molecular_functionhydrolase activity
E0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
E0097510biological_processbase-excision repair, AP site formation via deaminated base removal
F0005515molecular_functionprotein binding
G0004844molecular_functionuracil DNA N-glycosylase activity
G0005737cellular_componentcytoplasm
G0006281biological_processDNA repair
G0006284biological_processbase-excision repair
G0016787molecular_functionhydrolase activity
G0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
G0097510biological_processbase-excision repair, AP site formation via deaminated base removal
H0005515molecular_functionprotein binding
I0004844molecular_functionuracil DNA N-glycosylase activity
I0005737cellular_componentcytoplasm
I0006281biological_processDNA repair
I0006284biological_processbase-excision repair
I0016787molecular_functionhydrolase activity
I0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
I0097510biological_processbase-excision repair, AP site formation via deaminated base removal
J0005515molecular_functionprotein binding
K0004844molecular_functionuracil DNA N-glycosylase activity
K0005737cellular_componentcytoplasm
K0006281biological_processDNA repair
K0006284biological_processbase-excision repair
K0016787molecular_functionhydrolase activity
K0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
K0097510biological_processbase-excision repair, AP site formation via deaminated base removal
L0005515molecular_functionprotein binding
M0004844molecular_functionuracil DNA N-glycosylase activity
M0005737cellular_componentcytoplasm
M0006281biological_processDNA repair
M0006284biological_processbase-excision repair
M0016787molecular_functionhydrolase activity
M0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
M0097510biological_processbase-excision repair, AP site formation via deaminated base removal
N0005515molecular_functionprotein binding
Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. RVLIvGQDPY
ChainResidueDetails
AARG61-TYR70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASP68
CASP68
EASP68
GASP68
IASP68
KASP68
MASP68

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
AASP68
AHIS191

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
CASP68
CHIS191

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
EASP68
EHIS191

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
GASP68
GHIS191

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
IASP68
IHIS191

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
KASP68
KHIS191

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
MASP68
MHIS191

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon