6FW2
Crystal Structure of human mARC1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0030151 | molecular_function | molybdenum ion binding |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue MTE A 1201 |
| Chain | Residue |
| A | LYS67 |
| A | LEU214 |
| A | PHE237 |
| A | ARG238 |
| A | ASN240 |
| A | CYS270 |
| A | SER271 |
| A | CYS273 |
| A | TYR317 |
| A | EFK1202 |
| A | HOH1359 |
| A | SER68 |
| A | HOH1426 |
| A | HOH1536 |
| A | ASP91 |
| A | ARG92 |
| A | ASP209 |
| A | THR210 |
| A | SER211 |
| A | PRO212 |
| A | PHE213 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EFK A 1202 |
| Chain | Residue |
| A | SER271 |
| A | ARG272 |
| A | CYS273 |
| A | THR276 |
| A | MTE1201 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue B3P A 1203 |
| Chain | Residue |
| A | GLU1011 |
| A | ASP1020 |
| A | GLY1030 |
| A | HIS1031 |
| A | LEU1032 |
| A | ASP1070 |
| A | PHE1104 |
| A | GLN1105 |
| A | ARG1145 |
| A | HOH1317 |
| A | HOH1320 |
| A | HOH1340 |
| A | HOH1365 |
| A | HOH1369 |
| A | HOH1398 |
| A | HOH1416 |
| A | HOH1477 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MOO A 1204 |
| Chain | Residue |
| A | ARG1014 |
| A | LEU1015 |
| A | LYS1016 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MOO A 1205 |
| Chain | Residue |
| A | GLY1113 |
| A | PHE1114 |
| A | THR1115 |
| A | ASN1116 |
| A | SER1117 |
| A | ASN1132 |
| A | HOH1417 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue MOO A 1206 |
| Chain | Residue |
| A | ARG188 |
| A | TRP1126 |
| A | HOH1301 |
| A | HOH1304 |
| A | HOH1305 |
| A | HOH1450 |
| A | HOH1458 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MOO A 1207 |
| Chain | Residue |
| A | THR1142 |
| A | PRO1143 |
| A | ASN1144 |
| A | ARG1145 |
| A | HOH1379 |
| A | HOH1491 |
| A | HOH1506 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 1208 |
| Chain | Residue |
| A | ARG200 |
| A | PRO201 |
| A | LYS202 |
| A | HOH1374 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 148 |
| Details | Domain: {"description":"MOSC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00670","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30397129","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FW2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| A | GLU1011 | proton shuttle (general acid/base) |
| A | ASP1020 | covalent catalysis |
