3ZUR
Crystal structure of an engineered botulinum neurotoxin type A- SNARE23 derivative, LC0-A-SNAP25-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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1943 |
| Chain | Residue |
| A | LYS364 |
| A | ASN938 |
| A | GLN939 |
| A | ARG940 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1944 |
| Chain | Residue |
| A | LEU173 |
| A | ASN174 |
| A | ASN178 |
| A | LYS289 |
| A | HOH2030 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1939 |
| Chain | Residue |
| B | LEU173 |
| B | ASN174 |
| B | ASN178 |
| B | LYS289 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1945 |
| Chain | Residue |
| A | ILE910 |
| A | GLY911 |
| A | GLN912 |
| A | VAL913 |
| A | ASP914 |
| B | TYR903 |
| B | ARG906 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1946 |
| Chain | Residue |
| A | TYR903 |
| A | ARG906 |
| B | LYS900 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| B | ILE706-LEU726 | |
| A | ILE706-LEU726 | |
| A | LEU735-LEU755 | |
| B | LEU735-LEU755 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095 |
| Chain | Residue | Details |
| A | GLN224 | |
| B | GLN224 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 |
| B | HIS223 | |
| B | TYR227 | |
| A | HIS223 | |
| A | TYR227 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:11827515 |
| Chain | Residue | Details |
| B | ARG363 | |
| B | TYR366 | |
| A | ARG363 | |
| A | TYR366 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:9886085 |
| Chain | Residue | Details |
| A | ARG483 | |
| B | ARG483 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:9886085, ECO:0000305|PubMed:15592454 |
| Chain | Residue | Details |
| A | GLN500 | |
| B | GLN500 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C) => ECO:0000269|PubMed:9886085, ECO:0000305|PubMed:15592454 |
| Chain | Residue | Details |
| A | ARG501 | |
| B | ARG501 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60879 |
| Chain | Residue | Details |
| A | SER457 | |
| A | SER490 | |
| B | SER457 | |
| B | SER490 |
