1CY1
COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'PTPTPT
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 700 |
Chain | Residue |
A | ARG202 |
A | ALA458 |
A | ARG535 |
A | ASN539 |
A | HOH831 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TMP A 600 |
Chain | Residue |
A | GLN165 |
A | ARG168 |
A | HIS365 |
A | ARG493 |
A | SER495 |
A | ALA554 |
A | ASP113 |
A | ARG114 |
A | GLU115 |
A | ARG161 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE THP A 601 |
Chain | Residue |
A | ALA292 |
A | ARG296 |
A | LEU393 |
A | ARG396 |
A | GLN397 |
A | TRP434 |
A | MET438 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TMP A 602 |
Chain | Residue |
A | GLN291 |
A | SER294 |
A | THR295 |
A | SER478 |
A | SER481 |
A | ARG516 |
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 | 5 |
Details | Region: {"description":"Interaction with DNA"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21482796","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8114910","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9497321","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00952","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | Site: {"description":"Interaction with DNA"} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ecl |
Chain | Residue | Details |
A | ASP111 | |
A | TYR319 | |
A | GLU9 | |
A | HIS365 |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 366 |
Chain | Residue | Details |
A | GLU9 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor, proton relay |
A | ASP111 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor, proton relay |
A | ASP113 | metal ligand |
A | GLU115 | metal ligand |
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 |