3BTA
CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004222 | molecular_function | metalloendopeptidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008320 | molecular_function | protein transmembrane transporter activity |
A | 0016020 | cellular_component | membrane |
A | 0020002 | cellular_component | host cell plasma membrane |
A | 0030430 | cellular_component | host cell cytoplasm |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0044161 | cellular_component | host cell cytoplasmic vesicle |
A | 0044164 | cellular_component | host cell cytosol |
A | 0044221 | cellular_component | host cell synapse |
A | 0044231 | cellular_component | host cell presynaptic membrane |
A | 0046872 | molecular_function | metal ion binding |
A | 0071806 | biological_process | protein transmembrane transport |
A | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 1311 |
Chain | Residue |
A | HIS222 |
A | HIS226 |
A | GLU261 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLAHELIHAG |
Chain | Residue | Details |
A | THR219-GLY228 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | ALA627-TYR647 | |
A | ILE656-GLY676 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095 |
Chain | Residue | Details |
A | LEU224 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0000305|PubMed:9783750, ECO:0007744|PDB:2NYY, ECO:0007744|PDB:2NZ9, ECO:0007744|PDB:3BTA, ECO:0007744|PDB:3QIX, ECO:0007744|PDB:3QIY, ECO:0007744|PDB:3QIZ, ECO:0007744|PDB:3QJ0 |
Chain | Residue | Details |
A | GLU223 | |
A | ALA227 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0007744|PDB:2NYY, ECO:0007744|PDB:2NZ9, ECO:0007744|PDB:3BTA, ECO:0007744|PDB:3QIX, ECO:0007744|PDB:3QIY, ECO:0007744|PDB:3QIZ, ECO:0007744|PDB:3QJ0 |
Chain | Residue | Details |
A | LEU262 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18704164, ECO:0000269|PubMed:27958736, ECO:0007744|PDB:2VU9, ECO:0007744|PDB:5TPB, ECO:0007744|PDB:5TPC |
Chain | Residue | Details |
A | ASP1117 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18704164, ECO:0000269|PubMed:27958736, ECO:0000305|PubMed:14731268, ECO:0007744|PDB:2VU9, ECO:0007744|PDB:5TPB, ECO:0007744|PDB:5TPC |
Chain | Residue | Details |
A | LYS1203 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:11827515 |
Chain | Residue | Details |
A | LYS363 | |
A | LEU366 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1i1e |
Chain | Residue | Details |
A | ARG362 | |
A | GLU261 | |
A | TYR365 |