5VBA
Structure of EspG1 chaperone from the type VII (ESX-1) secretion system determined with the assistance of N-terminal T4 lysozyme fusion
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| 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 |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0009253 | biological_process | peptidoglycan catabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 1201 |
| Chain | Residue |
| A | HIS73 |
| A | THR1021 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 1202 |
| Chain | Residue |
| A | PHE1114 |
| A | SER1117 |
| A | ASN1132 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 1203 |
| Chain | Residue |
| B | ARG101 |
| A | ARG1125 |
| A | TRP1126 |
| A | ASP1127 |
| A | GLU1128 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 1204 |
| Chain | Residue |
| A | THR1142 |
| A | ASN1144 |
| A | ARG1145 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 1205 |
| Chain | Residue |
| A | LYS217 |
| A | ALA218 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 1201 |
| Chain | Residue |
| A | GLN1000 |
| B | ASN1002 |
| B | ILE1003 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 1202 |
| Chain | Residue |
| B | ALA136 |
| B | PRO137 |
| B | GLN138 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 1203 |
| Chain | Residue |
| B | LYS217 |
| B | ALA218 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 1204 |
| Chain | Residue |
| B | THR1142 |
| B | ASN1144 |
| B | ARG1145 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 1205 |
| Chain | Residue |
| B | PHE1114 |
| B | THR1115 |
| B | ASN1116 |
| B | HOH1321 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | GLU1011 | |
| B | GLU1011 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | ASP1020 | |
| B | ASP1020 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | LEU1032 | |
| A | PHE1104 | |
| B | LEU1032 | |
| B | PHE1104 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
| Chain | Residue | Details |
| A | SER1117 | |
| A | ASN1132 | |
| B | SER1117 | |
| B | ASN1132 |
