1MW9
Crystal Structure of H365R mutant of 67 kDA N-terminal fragment of E. coli DNA Topoisomerase I
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2001 |
| Chain | Residue |
| X | ARG114 |
| X | ARG161 |
| X | HOH1273 |
| X | HOH1447 |
| X | HOH1465 |
| X | HOH1550 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2002 |
| Chain | Residue |
| X | TRP220 |
| X | LYS251 |
| X | HOH1148 |
| X | HOH1184 |
| X | HOH1200 |
| X | HOH1416 |
| X | PRO11 |
| X | LYS28 |
| X | SER29 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2003 |
| Chain | Residue |
| X | PRO87 |
| X | GLY88 |
| X | LYS89 |
| X | GLU90 |
| X | HOH1124 |
| X | HOH1233 |
| X | HOH1253 |
| X | HOH1317 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2004 |
| Chain | Residue |
| X | TRP560 |
| X | LYS561 |
| X | HOH1119 |
| X | HOH1145 |
| X | HOH1173 |
| X | HOH1248 |
| X | HOH1271 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2005 |
| Chain | Residue |
| X | ARG515 |
| X | ARG516 |
| X | HOH1161 |
| X | HOH1165 |
| X | HOH1289 |
| X | HOH1502 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2006 |
| Chain | Residue |
| X | LYS436 |
| X | ALA440 |
| X | HIS556 |
| X | HOH1188 |
| X | HOH1209 |
| X | HOH1267 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2007 |
| Chain | Residue |
| X | ARG202 |
| X | ALA458 |
| X | ARG535 |
| X | ASN539 |
| X | HOH1005 |
| X | HOH1011 |
| X | HOH1359 |
| X | HOH1400 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2008 |
| Chain | Residue |
| X | GLN468 |
| X | HIS469 |
| X | PHE470 |
| X | LYS472 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 X 2009 |
| Chain | Residue |
| X | ASP113 |
| X | ARG114 |
| X | SER495 |
| X | HOH1013 |
| X | HOH1069 |
| X | HOH1086 |
| X | HOH1206 |
| X | HOH1350 |
| X | HOH1550 |
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 |
| X | 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 |
| X | TYR319 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00952 |
| Chain | Residue | Details |
| X | GLU9 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| X | ASP111 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Interaction with DNA |
| Chain | Residue | Details |
| X | HIS33 | |
| X | ARG168 | |
| X | ARG169 | |
| X | ASP172 | |
| X | TYR177 | |
| X | TRP184 | |
| X | ARG321 | |
| X | ARG507 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ecl |
| Chain | Residue | Details |
| X | ASP111 | |
| X | TYR319 | |
| X | GLU9 | |
| X | ARG365 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 366 |
| Chain | Residue | Details |
| X | GLU9 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor, proton relay |
| X | ASP111 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor, proton relay |
| X | ASP113 | metal ligand |
| X | GLU115 | metal ligand |
| X | TYR319 | activator, covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, proton acceptor, proton donor |
| X | ARG321 | electrostatic stabiliser |
| X | ARG365 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, proton acceptor, proton donor |
