2ABK
REFINEMENT OF THE NATIVE STRUCTURE OF ENDONUCLEASE III TO A RESOLUTION OF 1.85 ANGSTROM
Replaces: 1ABKFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000703 | molecular_function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity |
A | 0003677 | molecular_function | DNA binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
A | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
A | 0005515 | molecular_function | protein binding |
A | 0006281 | biological_process | DNA repair |
A | 0006284 | biological_process | base-excision repair |
A | 0006285 | biological_process | base-excision repair, AP site formation |
A | 0006950 | biological_process | response to stress |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016829 | molecular_function | lyase activity |
A | 0019104 | molecular_function | DNA N-glycosylase activity |
A | 0034644 | biological_process | cellular response to UV |
A | 0046872 | molecular_function | metal ion binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
A | 0097510 | biological_process | base-excision repair, AP site formation via deaminated base removal |
A | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from PDB Data
site_id | 1 |
Number of Residues | 2 |
Details | DNA GLYCOSYLASE AND DNA LYASE ACTIVITY |
Chain | Residue |
A | LYS120 |
A | ASP138 |
site_id | 2 |
Number of Residues | 1 |
Details | DNA BINDING |
Chain | Residue |
A | LYS191 |
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 A 300 |
Chain | Residue |
A | CYS203 |
A | TYR205 |
A | THR148 |
A | HIS182 |
A | CYS187 |
A | CYS194 |
A | CYS197 |
A | GLU200 |
Functional Information from PROSITE/UniProt
site_id | PS00764 |
Number of Residues | 17 |
Details | ENDONUCLEASE_III_1 Endonuclease III iron-sulfur binding region signature. CiarKPRCgsCiiedlC |
Chain | Residue | Details |
A | CYS187-CYS203 |
site_id | PS01155 |
Number of Residues | 30 |
Details | ENDONUCLEASE_III_2 Endonuclease III family signature. GeVPedraaLea.LPGVGrktAnvvLntAFG |
Chain | Residue | Details |
A | GLY102-GLY131 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7664751, ECO:0007744|PDB:2ABK |
Chain | Residue | Details |
A | CYS187 | |
A | CYS194 | |
A | CYS197 | |
A | CYS203 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 1411536, 7664751, 7806489, 10467137, 11695910 |
Chain | Residue | Details |
A | ASP138 | |
A | LYS120 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 888 |
Chain | Residue | Details |
A | LYS120 | covalent catalysis |
A | ASP138 | proton shuttle (general acid/base) |