3A18
Crystal Structure of Aldoxime Dehydratase (OxdRE) in Complex with Butyraldoxime (soaked crystal)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0016829 | molecular_function | lyase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0016829 | molecular_function | lyase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0016829 | molecular_function | lyase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM A 354 |
Chain | Residue |
A | PHE27 |
A | SER219 |
A | ILE238 |
A | LEU242 |
A | MET246 |
A | ASN279 |
A | LEU289 |
A | TRP292 |
A | SER293 |
A | HIS299 |
A | ILE302 |
A | HIS169 |
A | PHE306 |
A | BXO355 |
A | HOH372 |
A | HOH444 |
A | HOH514 |
A | GLY170 |
A | TYR171 |
A | TRP172 |
A | GLY173 |
A | SER174 |
A | MET175 |
A | ILE217 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BXO A 355 |
Chain | Residue |
A | MET29 |
A | SER219 |
A | HIS320 |
A | HEM354 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 354 |
Chain | Residue |
B | PHE27 |
B | HIS169 |
B | GLY170 |
B | TYR171 |
B | TRP172 |
B | GLY173 |
B | SER174 |
B | MET175 |
B | SER219 |
B | ILE238 |
B | MET246 |
B | ASN279 |
B | LEU289 |
B | TRP292 |
B | SER293 |
B | HIS299 |
B | ILE302 |
B | PHE306 |
B | PHE307 |
B | BXO355 |
B | HOH396 |
B | HOH480 |
B | HOH528 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BXO B 355 |
Chain | Residue |
B | MET29 |
B | SER219 |
B | TYR319 |
B | HIS320 |
B | HEM354 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM C 354 |
Chain | Residue |
C | PHE27 |
C | HIS169 |
C | GLY170 |
C | TYR171 |
C | TRP172 |
C | GLY173 |
C | SER174 |
C | MET175 |
C | ILE217 |
C | SER219 |
C | ILE238 |
C | LEU242 |
C | MET246 |
C | ASN279 |
C | LEU289 |
C | TRP292 |
C | SER293 |
C | HIS299 |
C | ILE302 |
C | PHE306 |
C | BXO355 |
C | HOH421 |
C | HOH438 |
D | HOH816 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BXO C 355 |
Chain | Residue |
C | SER219 |
C | HIS320 |
C | HEM354 |
site_id | AC7 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM D 354 |
Chain | Residue |
D | HIS299 |
D | ILE302 |
D | PHE303 |
D | PHE306 |
D | LEU318 |
D | BXO355 |
D | HOH371 |
D | HOH389 |
D | HOH694 |
D | PHE27 |
D | HIS169 |
D | GLY170 |
D | TYR171 |
D | TRP172 |
D | GLY173 |
D | SER174 |
D | MET175 |
D | SER219 |
D | ILE238 |
D | LEU242 |
D | MET246 |
D | ASN279 |
D | LEU289 |
D | TRP292 |
D | SER293 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BXO D 355 |
Chain | Residue |
D | SER219 |
D | TYR319 |
D | HIS320 |
D | HEM354 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:19740758 |
Chain | Residue | Details |
A | HIS320 | |
B | HIS320 | |
C | HIS320 | |
D | HIS320 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19740758, ECO:0007744|PDB:3A16, ECO:0007744|PDB:3A17, ECO:0007744|PDB:3A18 |
Chain | Residue | Details |
A | SER219 | |
A | HIS320 | |
B | SER219 | |
B | HIS320 | |
C | SER219 | |
C | HIS320 | |
D | SER219 | |
D | HIS320 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:19740758, ECO:0007744|PDB:3A15, ECO:0007744|PDB:3A16, ECO:0007744|PDB:3A17, ECO:0007744|PDB:3A18 |
Chain | Residue | Details |
A | HIS299 | |
B | HIS299 | |
C | HIS299 | |
D | HIS299 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 361 |
Chain | Residue | Details |
A | GLU143 | hydrogen bond acceptor, steric role |
A | ARG178 | hydrogen bond donor, steric role |
A | SER219 | hydrogen bond acceptor, steric role |
A | HIS299 | metal ligand, steric role |
A | PHE306 | steric role |
A | HIS320 | activator, hydrogen bond acceptor, hydrogen bond donor, promote heterolysis, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 361 |
Chain | Residue | Details |
B | GLU143 | hydrogen bond acceptor, steric role |
B | ARG178 | hydrogen bond donor, steric role |
B | SER219 | hydrogen bond acceptor, steric role |
B | HIS299 | metal ligand, steric role |
B | PHE306 | steric role |
B | HIS320 | activator, hydrogen bond acceptor, hydrogen bond donor, promote heterolysis, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 361 |
Chain | Residue | Details |
C | GLU143 | hydrogen bond acceptor, steric role |
C | ARG178 | hydrogen bond donor, steric role |
C | SER219 | hydrogen bond acceptor, steric role |
C | HIS299 | metal ligand, steric role |
C | PHE306 | steric role |
C | HIS320 | activator, hydrogen bond acceptor, hydrogen bond donor, promote heterolysis, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 361 |
Chain | Residue | Details |
D | GLU143 | hydrogen bond acceptor, steric role |
D | ARG178 | hydrogen bond donor, steric role |
D | SER219 | hydrogen bond acceptor, steric role |
D | HIS299 | metal ligand, steric role |
D | PHE306 | steric role |
D | HIS320 | activator, hydrogen bond acceptor, hydrogen bond donor, promote heterolysis, proton acceptor, proton donor |