Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016020 | cellular_component | membrane |
A | 0016192 | biological_process | vesicle-mediated transport |
B | 0005484 | molecular_function | SNAP receptor activity |
B | 0006886 | biological_process | intracellular protein transport |
B | 0016020 | cellular_component | membrane |
B | 0016192 | biological_process | vesicle-mediated transport |
C | 0000149 | molecular_function | SNARE binding |
C | 0005249 | molecular_function | voltage-gated potassium channel activity |
C | 0017075 | molecular_function | syntaxin-1 binding |
E | 0016020 | cellular_component | membrane |
F | 0016020 | cellular_component | membrane |
G | 0016020 | cellular_component | membrane |
G | 0016192 | biological_process | vesicle-mediated transport |
H | 0005484 | molecular_function | SNAP receptor activity |
H | 0006886 | biological_process | intracellular protein transport |
H | 0016020 | cellular_component | membrane |
H | 0016192 | biological_process | vesicle-mediated transport |
I | 0000149 | molecular_function | SNARE binding |
I | 0005249 | molecular_function | voltage-gated potassium channel activity |
I | 0017075 | molecular_function | syntaxin-1 binding |
K | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | binding site for residue CA C 102 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA E 501 |
Chain | Residue |
E | ASP303 |
E | ASP309 |
E | ASP363 |
E | TYR364 |
E | ASP365 |
E | CA502 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CA E 502 |
Chain | Residue |
E | ASP363 |
E | ASP365 |
E | CA501 |
E | MET302 |
E | ASP303 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CA E 503 |
Chain | Residue |
E | ASP172 |
E | ASP230 |
E | PHE231 |
E | ASP232 |
E | CA504 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CA E 504 |
Chain | Residue |
E | ASP172 |
E | ASP178 |
E | ASP230 |
E | PHE231 |
E | CA503 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue CA F 501 |
Chain | Residue |
F | ASP172 |
F | ASP178 |
F | ASP230 |
F | PHE231 |
F | CA504 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue CA F 502 |
Chain | Residue |
F | ASP172 |
F | ASP230 |
F | ASP232 |
F | LYS324 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CA F 503 |
Chain | Residue |
F | ASP303 |
F | ASP309 |
F | ASP363 |
F | TYR364 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue CA F 504 |
Chain | Residue |
F | ASP172 |
F | THR176 |
F | SER177 |
F | ASP178 |
F | CA501 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue CA K 501 |
Chain | Residue |
K | MET302 |
K | ASP303 |
K | LEU307 |
K | SER308 |
K | ASP363 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue CA K 502 |
Chain | Residue |
K | ASP303 |
K | ASP309 |
K | ASP363 |
K | TYR364 |
K | ASP365 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue CA K 503 |
Chain | Residue |
K | ASP172 |
K | ASP230 |
K | PHE231 |
K | ASP232 |
K | CA504 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue CA K 504 |
Chain | Residue |
E | GLU346 |
K | ASP172 |
K | ASP178 |
K | PHE231 |
K | CA503 |
Functional Information from PROSITE/UniProt
site_id | PS00417 |
Number of Residues | 20 |
Details | SYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD |
Chain | Residue | Details |
A | ASN49-ASP68 | |
site_id | PS00914 |
Number of Residues | 40 |
Details | SYNTAXIN Syntaxin / epimorphin family signature. RhseIikLEnsIrELhdMFmdMamlVesQGemIDrIEyn.V |
Chain | Residue | Details |
B | ARG198-VAL237 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
E | LEU171 | |
E | ASP303 | |
E | ASP309 | |
E | ASP363 | |
E | ASP365 | |
E | ASP371 | |
F | LEU171 | |
F | ASP172 | |
F | ASP178 | |
F | ASP230 | |
F | PHE231 | |
E | ASP172 | |
F | ASP232 | |
F | SER235 | |
F | LYS236 | |
F | ASP238 | |
F | ASP303 | |
F | ASP309 | |
F | ASP363 | |
F | ASP365 | |
F | ASP371 | |
K | LEU171 | |
E | ASP178 | |
K | ASP172 | |
K | ASP178 | |
K | ASP230 | |
K | PHE231 | |
K | ASP232 | |
K | SER235 | |
K | LYS236 | |
K | ASP238 | |
K | ASP303 | |
K | ASP309 | |
E | ASP230 | |
K | ASP363 | |
K | ASP365 | |
K | ASP371 | |
E | PHE231 | |
E | ASP232 | |
E | SER235 | |
E | LYS236 | |
E | ASP238 | |
Chain | Residue | Details |
E | TYR229 | |
F | TYR229 | |
K | TYR229 | |
B | LYS256 | |
H | LYS252 | |
H | LYS253 | |
H | LYS256 | |
Chain | Residue | Details |
E | SER264 | |
F | SER264 | |
K | SER264 | |
Chain | Residue | Details |
E | SER342 | |
E | SER344 | |
F | SER342 | |
F | SER344 | |
K | SER342 | |
K | SER344 | |