2ZHX

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004844	molecular_function	uracil DNA N-glycosylase activity
A	0005737	cellular_component	cytoplasm
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0006974	biological_process	DNA damage response
A	0016787	molecular_function	hydrolase activity
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
A	0097510	biological_process	base-excision repair, AP site formation via deaminated base removal
B	0005515	molecular_function	protein binding
C	0004844	molecular_function	uracil DNA N-glycosylase activity
C	0005737	cellular_component	cytoplasm
C	0006281	biological_process	DNA repair
C	0006284	biological_process	base-excision repair
C	0006974	biological_process	DNA damage response
C	0016787	molecular_function	hydrolase activity
C	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
C	0097510	biological_process	base-excision repair, AP site formation via deaminated base removal
D	0005515	molecular_function	protein binding
E	0004844	molecular_function	uracil DNA N-glycosylase activity
E	0005737	cellular_component	cytoplasm
E	0006281	biological_process	DNA repair
E	0006284	biological_process	base-excision repair
E	0006974	biological_process	DNA damage response
E	0016787	molecular_function	hydrolase activity
E	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
E	0097510	biological_process	base-excision repair, AP site formation via deaminated base removal
F	0005515	molecular_function	protein binding
G	0004844	molecular_function	uracil DNA N-glycosylase activity
G	0005737	cellular_component	cytoplasm
G	0006281	biological_process	DNA repair
G	0006284	biological_process	base-excision repair
G	0006974	biological_process	DNA damage response
G	0016787	molecular_function	hydrolase activity
G	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
G	0097510	biological_process	base-excision repair, AP site formation via deaminated base removal
H	0005515	molecular_function	protein binding
I	0004844	molecular_function	uracil DNA N-glycosylase activity
I	0005737	cellular_component	cytoplasm
I	0006281	biological_process	DNA repair
I	0006284	biological_process	base-excision repair
I	0006974	biological_process	DNA damage response
I	0016787	molecular_function	hydrolase activity
I	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
I	0097510	biological_process	base-excision repair, AP site formation via deaminated base removal
J	0005515	molecular_function	protein binding
K	0004844	molecular_function	uracil DNA N-glycosylase activity
K	0005737	cellular_component	cytoplasm
K	0006281	biological_process	DNA repair
K	0006284	biological_process	base-excision repair
K	0006974	biological_process	DNA damage response
K	0016787	molecular_function	hydrolase activity
K	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
K	0097510	biological_process	base-excision repair, AP site formation via deaminated base removal
L	0005515	molecular_function	protein binding
M	0004844	molecular_function	uracil DNA N-glycosylase activity
M	0005737	cellular_component	cytoplasm
M	0006281	biological_process	DNA repair
M	0006284	biological_process	base-excision repair
M	0006974	biological_process	DNA damage response
M	0016787	molecular_function	hydrolase activity
M	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
M	0097510	biological_process	base-excision repair, AP site formation via deaminated base removal
N	0005515	molecular_function	protein binding

Functional Information from PROSITE/UniProt

site_id	PS00130
Number of Residues	10
Details	U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. RVLIvGQDPY

Chain	Residue	Details
A	ARG61-TYR70

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1eug

Chain	Residue	Details
A	ASP68
A	HIS191

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1eug

Chain	Residue	Details
C	ASP68
C	HIS191

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1eug

Chain	Residue	Details
E	ASP68
E	HIS191

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1eug

Chain	Residue	Details
G	ASP68
G	HIS191

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1eug

Chain	Residue	Details
I	ASP68
I	HIS191

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1eug

Chain	Residue	Details
K	ASP68
K	HIS191

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1eug

Chain	Residue	Details
M	ASP68
M	HIS191

---