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 | 0016020 | cellular_component | membrane |
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 | 0016020 | cellular_component | membrane |
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 | 0016020 | cellular_component | membrane |
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 | 0016020 | cellular_component | membrane |
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 | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22819216 |
Chain | Residue | Details |
A | LYS185 | |
C | SER227 | |
C | TYR233 | |
C | TYR282 | |
D | LYS185 | |
D | SER227 | |
D | TYR233 | |
D | TYR282 | |
A | SER227 | |
A | TYR233 | |
A | TYR282 | |
B | LYS185 | |
B | SER227 | |
B | TYR233 | |
B | TYR282 | |
C | LYS185 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | SITE: Crucial for binding sphingomyelin and inducing hemolysis => ECO:0000269|PubMed:15274631 |
Chain | Residue | Details |
A | TRP20 | |
D | TRP20 | |
D | TRP245 | |
D | TRP291 | |
A | TRP245 | |
A | TRP291 | |
B | TRP20 | |
B | TRP245 | |
B | TRP291 | |
C | TRP20 | |
C | TRP245 | |
C | TRP291 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Crucial for binding sphingomyelin and important for inducing hemolysis => ECO:0000269|PubMed:15274631 |
Chain | Residue | Details |
A | TRP187 | |
B | TRP187 | |
C | TRP187 | |
D | TRP187 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Important for activity |
Chain | Residue | Details |
A | PHE209 | |
B | PHE209 | |
C | PHE209 | |
D | PHE209 |