1IAZ
EQUINATOXIN II
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006812 | biological_process | monoatomic cation transport |
| A | 0015267 | molecular_function | channel activity |
| 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 | 0042151 | cellular_component | nematocyst |
| A | 0044218 | cellular_component | other organism cell membrane |
| A | 0046930 | cellular_component | pore complex |
| A | 0046931 | biological_process | pore complex assembly |
| A | 0051715 | biological_process | cytolysis in another organism |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0090729 | molecular_function | toxin activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006812 | biological_process | monoatomic cation transport |
| B | 0015267 | molecular_function | channel activity |
| 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 | 0042151 | cellular_component | nematocyst |
| B | 0044218 | cellular_component | other organism cell membrane |
| B | 0046930 | cellular_component | pore complex |
| B | 0046931 | biological_process | pore complex assembly |
| B | 0051715 | biological_process | cytolysis in another organism |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | LYS123 |
| A | HOH488 |
| B | ARG120 |
| B | TYR122 |
| B | LYS123 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | HOH457 |
| A | HOH460 |
| B | ARG120 |
| A | ARG120 |
| A | TYR122 |
| A | LYS123 |
| A | HOH436 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| B | ASN147 |
| B | ASN165 |
| B | SER166 |
| B | SER167 |
| B | HOH412 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 403 |
| Chain | Residue |
| A | LYS30 |
| A | HOH480 |
| A | HOH555 |
| B | ARG53 |
| B | GLN130 |
| B | TYR133 |
| B | TYR138 |
| B | HOH508 |
| B | HOH561 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 B 404 |
| Chain | Residue |
| B | SER15 |
| B | PHE16 |
| B | ASN49 |
| B | GLU173 |
| B | HOH410 |
| B | HOH436 |
| B | HOH440 |
| B | HOH498 |
| B | HOH519 |
| B | HOH520 |
| B | HOH580 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 405 |
| Chain | Residue |
| A | ARG126 |
| A | ASP129 |
| A | ARG131 |
| A | HOH451 |
| B | ARG152 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 406 |
| Chain | Residue |
| A | ASN28 |
| A | VAL29 |
| A | LYS30 |
| A | LYS77 |
| A | HOH555 |
| B | TYR113 |
| B | TYR138 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 407 |
| Chain | Residue |
| A | ARG53 |
| A | TRP116 |
| A | TYR137 |
| A | HOH544 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 408 |
| Chain | Residue |
| A | ASN49 |
| A | ARG127 |
| A | ASN153 |
| A | HOH478 |
| A | HOH484 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 409 |
| Chain | Residue |
| B | LYS125 |
| B | ARG127 |
| B | ARG161 |
| B | HIS175 |
| B | SER177 |
| B | HOH450 |
| B | HOH523 |
| B | HOH581 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 410 |
| Chain | Residue |
| A | ARG53 |
| A | GLN130 |
| A | TYR133 |
| A | TYR138 |
| A | ARG144 |
| A | HOH508 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07845 |
| Chain | Residue | Details |
| A | SER54 | |
| B | SER105 | |
| B | PRO107 | |
| B | TYR133 | |
| B | TYR137 | |
| B | TYR138 | |
| A | VAL87 | |
| A | SER105 | |
| A | PRO107 | |
| A | TYR133 | |
| A | TYR137 | |
| A | TYR138 | |
| B | SER54 | |
| B | VAL87 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Important in the initial contact with the lipid membrane => ECO:0000269|PubMed:18442982 |
| Chain | Residue | Details |
| A | TRP112 | |
| A | TYR113 | |
| B | TRP112 | |
| B | TYR113 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Interacts with the lipid membrane => ECO:0000269|PubMed:18442982 |
| Chain | Residue | Details |
| A | ARG144 | |
| A | SER160 | |
| B | ARG144 | |
| B | SER160 |
