2END
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
Replaces: 1ENDFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000704 | molecular_function | pyrimidine dimer DNA N-glycosylase activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0006281 | biological_process | DNA repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 | Active site: {"description":"Nucleophile; via amide nitrogen","evidences":[{"source":"PubMed","id":"8347626","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VAS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"8347626","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VAS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Substrate binding","evidences":[{"source":"PubMed","id":"1409651","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7783199","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Substrate binding","evidences":[{"source":"PubMed","id":"1409651","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PDB","id":"1VAS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
