1ENI
CRYSTAL STRUCTURE OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME FROM BACTERIOPHAGE T4: REFINEMENT AT 1.45 ANGSTROMS AND X-RAY ANALYSIS OF THE THREE ACTIVE SITE MUTANTS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000704 | molecular_function | pyrimidine dimer DNA N-glycosylase activity |
A | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
A | 0004519 | molecular_function | endonuclease activity |
A | 0006281 | biological_process | DNA repair |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016829 | molecular_function | lyase activity |
A | 0033959 | molecular_function | deoxyribodipyrimidine endonucleosidase activity |
A | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile; via amide nitrogen => ECO:0000269|PubMed:8347626, ECO:0007744|PDB:1VAS |
Chain | Residue | Details |
A | THR2 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8347626, ECO:0007744|PDB:1VAS |
Chain | Residue | Details |
A | GLU23 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Substrate binding => ECO:0000269|PubMed:1409651, ECO:0000269|PubMed:7783199 |
Chain | Residue | Details |
A | GLN3 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | SITE: Substrate binding => ECO:0000269|PubMed:1409651 |
Chain | Residue | Details |
A | ARG22 | |
A | ARG117 | |
A | LYS121 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0007744|PDB:1VAS |
Chain | Residue | Details |
A | ARG26 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1vas |
Chain | Residue | Details |
A | ARG22 | |
A | THR2 | |
A | GLU23 | |
A | ARG26 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 162 |
Chain | Residue | Details |
A | THR2 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | ARG22 | electrostatic stabiliser, hydrogen bond donor |
A | GLU23 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG26 | electrostatic stabiliser, hydrogen bond donor |