2FCC
Crystal Structure of T4 Pyrimidine Dimer Glycosylase (T4-Pdg) Covalently Complexed with a DNA Substrate Containing Abasic Site
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 |
B | 0000704 | molecular_function | pyrimidine dimer DNA N-glycosylase activity |
B | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
B | 0004519 | molecular_function | endonuclease activity |
B | 0006281 | biological_process | DNA repair |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0016829 | molecular_function | lyase activity |
B | 0033959 | molecular_function | deoxyribodipyrimidine endonucleosidase activity |
B | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | THR49 |
A | PHE50 |
A | TYR104 |
A | PRO106 |
A | HIS107 |
A | SER110 |
A | HOH1080 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | GLN124 |
A | ARG117 |
A | LYS121 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 601 |
Chain | Residue |
B | THR49 |
B | PHE50 |
B | PHE59 |
B | TYR104 |
B | PRO106 |
B | HIS107 |
B | SER110 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 602 |
Chain | Residue |
A | PHE66 |
A | LYS69 |
A | ARG70 |
A | GLU73 |
A | HOH1044 |
A | HOH1088 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile; via amide nitrogen => ECO:0000269|PubMed:8347626, ECO:0007744|PDB:1VAS |
Chain | Residue | Details |
A | THR2 | |
B | THR2 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8347626, ECO:0007744|PDB:1VAS |
Chain | Residue | Details |
A | GLU23 | |
B | GLU23 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Substrate binding => ECO:0000269|PubMed:1409651, ECO:0000269|PubMed:7783199 |
Chain | Residue | Details |
A | ARG3 | |
B | ARG3 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Substrate binding => ECO:0000269|PubMed:1409651 |
Chain | Residue | Details |
A | ARG22 | |
A | ARG117 | |
A | LYS121 | |
B | ARG22 | |
B | ARG117 | |
B | LYS121 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0007744|PDB:1VAS |
Chain | Residue | Details |
A | ARG26 | |
B | 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 | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1vas |
Chain | Residue | Details |
B | ARG22 | |
B | THR2 | |
B | GLU23 | |
B | 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 |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 162 |
Chain | Residue | Details |
B | THR2 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | ARG22 | electrostatic stabiliser, hydrogen bond donor |
B | GLU23 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ARG26 | electrostatic stabiliser, hydrogen bond donor |