1LQM
ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006281 | biological_process | DNA repair |
A | 0006284 | biological_process | base-excision repair |
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 | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006281 | biological_process | DNA repair |
C | 0006284 | biological_process | base-excision repair |
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 | 0005515 | molecular_function | protein binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0006281 | biological_process | DNA repair |
E | 0006284 | biological_process | base-excision repair |
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 | 0005515 | molecular_function | protein binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0006281 | biological_process | DNA repair |
G | 0006284 | biological_process | base-excision repair |
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 |
Functional Information from PROSITE/UniProt
site_id | PS00130 |
Number of Residues | 10 |
Details | U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY |
Chain | Residue | Details |
A | LYS57-TYR66 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | PRO65 | |
C | PRO65 | |
E | PRO65 | |
G | PRO65 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eug |
Chain | Residue | Details |
A | HIS187 | |
A | ASP64 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eug |
Chain | Residue | Details |
C | HIS187 | |
C | ASP64 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eug |
Chain | Residue | Details |
E | HIS187 | |
E | ASP64 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eug |
Chain | Residue | Details |
G | HIS187 | |
G | ASP64 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 71 |
Chain | Residue | Details |
A | PRO65 | activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor |
A | HIS67 | activator, steric role |
A | SER78 | activator, steric role |
A | PRO188 | covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 71 |
Chain | Residue | Details |
C | PRO65 | activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor |
C | HIS67 | activator, steric role |
C | SER78 | activator, steric role |
C | PRO188 | covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 71 |
Chain | Residue | Details |
E | PRO65 | activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor |
E | HIS67 | activator, steric role |
E | SER78 | activator, steric role |
E | PRO188 | covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 71 |
Chain | Residue | Details |
G | PRO65 | activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor |
G | HIS67 | activator, steric role |
G | SER78 | activator, steric role |
G | PRO188 | covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |