1ECL
AMINO TERMINAL 67KDA DOMAIN OF ESCHERICHIA COLI DNA TOPOISOMERASE I (RESIDUES 2-590 OF MATURE PROTEIN) CLONING ARTIFACT ADDS TWO RESIDUES TO THE AMINO-TERMINUS WHICH WERE NOT OBSERVED IN THE EXPERIMENTAL ELECTRON DENSITY (GLY-2, SER-1).
Functional Information from GO Data
Functional Information from PDB Data
| site_id | TY3 |
| Number of Residues | 1 |
| Details | ACTIVE SITE TYROSINE INVOLVED IN MAKING PHOSPHOTYROSINE COVALENT LINKAGE WITH DNA DURING CATALYSIS |
| Chain | Residue |
| A | TYR319 |
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 | 3 |
| Details | a catalytic site defined by CSA, PubMed 9497321, 8114910, 20210704, 11809772 |
| Chain | Residue | Details |
| A | TYR319 | |
| A | GLU9 | |
| A | ARG321 |
| 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 |
