1CY9
CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. MONOCLINIC FORM
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003916 | molecular_function | DNA topoisomerase activity |
A | 0003917 | molecular_function | DNA topoisomerase type I (single strand cut, ATP-independent) activity |
A | 0006265 | biological_process | DNA topological change |
B | 0003677 | molecular_function | DNA binding |
B | 0003916 | molecular_function | DNA topoisomerase activity |
B | 0003917 | molecular_function | DNA topoisomerase type I (single strand cut, ATP-independent) activity |
B | 0006265 | biological_process | DNA topological change |
Functional Information from PROSITE/UniProt
site_id | PS00396 |
Number of Residues | 15 |
Details | TOPO_IA_1 Topoisomerase (Topo) IA-type active site signature. QrLYEagy.........ITYmRTD |
Chain | Residue | Details |
A | GLN309-ASP323 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000269|PubMed:21482796, ECO:0000269|PubMed:8114910, ECO:0000269|PubMed:9497321 |
Chain | Residue | Details |
A | TYR319 | |
B | TYR319 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Interaction with DNA |
Chain | Residue | Details |
A | ARG321 | |
B | ARG321 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 366 |
Chain | Residue | Details |
A | TYR319 | activator, covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | ARG321 | electrostatic stabiliser |
A | HIS365 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 366 |
Chain | Residue | Details |
B | TYR319 | activator, covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | ARG321 | electrostatic stabiliser |
B | HIS365 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, proton acceptor, proton donor |