3ZUS
Crystal structure of an engineered botulinum neurotoxin type A- SNARE23 derivative, LC-A-SNAP23-Hn-A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008320 | molecular_function | protein transmembrane transporter activity |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008320 | molecular_function | protein transmembrane transporter activity |
| C | 0004222 | molecular_function | metalloendopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008320 | molecular_function | protein transmembrane transporter activity |
| D | 0004222 | molecular_function | metalloendopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008320 | molecular_function | protein transmembrane transporter activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A1916 |
| Chain | Residue |
| A | HIS223 |
| A | HIS227 |
| A | GLU262 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1916 |
| Chain | Residue |
| B | HIS223 |
| B | HIS227 |
| B | GLU262 |
| B | HOH2005 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C1916 |
| Chain | Residue |
| C | GLU262 |
| C | HIS223 |
| C | HIS227 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D1917 |
| Chain | Residue |
| D | HIS223 |
| D | HIS227 |
| D | GLU262 |
| D | HOH2003 |
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 | THR220-GLY229 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | ILE677-LEU697 | |
| A | LEU706-LEU726 | |
| B | ILE677-LEU697 | |
| B | LEU706-LEU726 | |
| C | ILE677-LEU697 | |
| C | LEU706-LEU726 | |
| D | ILE677-LEU697 | |
| D | LEU706-LEU726 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095 |
| Chain | Residue | Details |
| A | GLU224 | |
| B | GLU224 | |
| C | GLU224 | |
| D | GLU224 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| 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 | HIS223 | |
| A | HIS227 | |
| B | HIS223 | |
| B | HIS227 | |
| C | HIS223 | |
| C | HIS227 | |
| D | HIS223 | |
| D | HIS227 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | GLU262 | |
| B | GLU262 | |
| C | GLU262 | |
| D | GLU262 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:11827515 |
| Chain | Residue | Details |
| A | ARG363 | |
| A | TYR366 | |
| B | ARG363 | |
| B | TYR366 | |
| C | ARG363 | |
| C | TYR366 | |
| D | ARG363 | |
| D | TYR366 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER445 | |
| B | SER445 | |
| C | SER445 | |
| D | SER445 |
