3ZXD
wild-type lysenin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0044218 | cellular_component | other organism cell membrane |
| A | 0090729 | molecular_function | toxin activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0044218 | cellular_component | other organism cell membrane |
| B | 0090729 | molecular_function | toxin activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0031640 | biological_process | killing of cells of another organism |
| C | 0035821 | biological_process | modulation of process of another organism |
| C | 0042742 | biological_process | defense response to bacterium |
| C | 0044218 | cellular_component | other organism cell membrane |
| C | 0090729 | molecular_function | toxin activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0031640 | biological_process | killing of cells of another organism |
| D | 0035821 | biological_process | modulation of process of another organism |
| D | 0042742 | biological_process | defense response to bacterium |
| D | 0044218 | cellular_component | other organism cell membrane |
| D | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 398 |
| Chain | Residue |
| A | TYR225 |
| A | SER227 |
| A | ASP228 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 467 |
| Chain | Residue |
| A | ALA18 |
| A | SER151 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 921 |
| Chain | Residue |
| A | LYS249 |
| A | SER250 |
| A | PRO252 |
| A | ASP257 |
| A | THR63 |
| A | SER65 |
| A | ASP68 |
| A | ASN248 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 468 |
| Chain | Residue |
| B | ASN248 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES B 921 |
| Chain | Residue |
| B | THR63 |
| B | SER65 |
| B | ASP68 |
| B | ASN248 |
| B | LYS249 |
| B | SER250 |
| B | PRO252 |
| B | ASP257 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 398 |
| Chain | Residue |
| C | GLU22 |
| C | TYR24 |
| C | VAL25 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 546 |
| Chain | Residue |
| C | LYS249 |
| C | ASP257 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 467 |
| Chain | Residue |
| A | GLY30 |
| A | SER31 |
| D | TYR24 |
| D | MG470 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES D 921 |
| Chain | Residue |
| D | THR66 |
| D | ASP68 |
| D | LYS249 |
| D | SER250 |
| D | PRO252 |
| D | ASP257 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 466 |
| Chain | Residue |
| A | VAL14 |
| A | SER62 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 469 |
| Chain | Residue |
| A | SER186 |
| A | TRP187 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 468 |
| Chain | Residue |
| A | VAL19 |
| A | TRP20 |
| A | GLN147 |
| A | VAL148 |
| A | MG470 |
| B | TYR265 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 470 |
| Chain | Residue |
| A | SO4468 |
| B | LYS264 |
| B | TYR265 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA A 500 |
| Chain | Residue |
| A | GLN143 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 501 |
| Chain | Residue |
| A | GLU13 |
| A | ASP15 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 502 |
| Chain | Residue |
| A | GLU174 |
| A | LYS290 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 465 |
| Chain | Residue |
| B | VAL14 |
| B | ASP15 |
| B | ILE60 |
| B | SER62 |
| B | THR63 |
| B | MG470 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA B 500 |
| Chain | Residue |
| B | ALA18 |
| B | VAL148 |
| B | SER151 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 470 |
| Chain | Residue |
| B | SO4465 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 472 |
| Chain | Residue |
| B | SER59 |
| B | THR66 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 473 |
| Chain | Residue |
| B | TYR225 |
| B | SER227 |
| B | ASP228 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 547 |
| Chain | Residue |
| B | GLU76 |
| C | GLU22 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA D 500 |
| Chain | Residue |
| B | LYS42 |
| D | GLU102 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 470 |
| Chain | Residue |
| D | VAL25 |
| D | SO4467 |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. ETRTVTATHSI |
| Chain | Residue | Details |
| A | GLU50-ILE60 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 284 |
| Details | Region: {"description":"N-terminal cap domain","evidences":[{"source":"PubMed","id":"27048994","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 292 |
| Details | Region: {"description":"Beta-hairpin domain","evidences":[{"source":"PubMed","id":"27048994","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 420 |
| Details | Region: {"description":"C-terminal receptor-binding domain","evidences":[{"source":"PubMed","id":"27048994","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22819216","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Site: {"description":"Crucial for binding sphingomyelin and inducing hemolysis","evidences":[{"source":"PubMed","id":"15274631","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Crucial for binding sphingomyelin and important for inducing hemolysis","evidences":[{"source":"PubMed","id":"15274631","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for activity"} |
| Chain | Residue | Details |
