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 | 1 |
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 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00952 |
Chain | Residue | Details |
A | GLU9 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ASP111 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | SITE: Interaction with DNA |
Chain | Residue | Details |
A | HIS33 | |
A | ARG168 | |
A | ARG169 | |
A | ASP172 | |
A | TYR177 | |
A | TRP184 | |
A | ARG321 | |
A | ARG507 |
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 |