3A16
Crystal Structure of Aldoxime Dehydratase (OxdRE) in Complex with Propionaldoxime
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 | 25 |
Details | BINDING SITE FOR RESIDUE HEM A 354 |
Chain | Residue |
A | PHE27 |
A | ILE238 |
A | LEU242 |
A | MET246 |
A | ASN279 |
A | LEU289 |
A | TRP292 |
A | SER293 |
A | HIS299 |
A | ILE302 |
A | PHE306 |
A | HIS169 |
A | LEU318 |
A | PXO355 |
A | HOH363 |
A | HOH400 |
A | HOH415 |
A | HOH458 |
A | GLY170 |
A | TYR171 |
A | TRP172 |
A | GLY173 |
A | SER174 |
A | MET175 |
A | SER219 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PXO A 355 |
Chain | Residue |
A | SER219 |
A | TYR319 |
A | HIS320 |
A | HEM354 |
site_id | AC3 |
Number of Residues | 24 |
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 | ILE217 |
B | SER219 |
B | ILE238 |
B | MET246 |
B | ASN279 |
B | LEU289 |
B | TRP292 |
B | SER293 |
B | HIS299 |
B | ILE302 |
B | PHE303 |
B | PHE306 |
B | PXO355 |
B | HOH360 |
B | HOH361 |
B | HOH374 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PXO B 355 |
Chain | Residue |
B | SER219 |
B | TYR319 |
B | HIS320 |
B | HEM354 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 356 |
Chain | Residue |
B | HOH364 |
B | HOH416 |
B | HOH423 |
B | HOH451 |
B | HOH472 |
B | HOH480 |
site_id | AC6 |
Number of Residues | 21 |
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 | SER219 |
C | ILE238 |
C | LEU242 |
C | MET246 |
C | ASN279 |
C | LEU289 |
C | TRP292 |
C | SER293 |
C | HIS299 |
C | ILE302 |
C | PXO355 |
C | HOH392 |
C | HOH451 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PXO C 355 |
Chain | Residue |
C | SER219 |
C | HIS320 |
C | HEM354 |
site_id | AC8 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM D 354 |
Chain | Residue |
D | MET246 |
D | ASN279 |
D | LEU289 |
D | TRP292 |
D | SER293 |
D | HIS299 |
D | ILE302 |
D | PHE303 |
D | PHE306 |
D | PXO355 |
D | HOH358 |
D | HOH361 |
D | HOH393 |
D | PHE27 |
D | HIS169 |
D | GLY170 |
D | TYR171 |
D | TRP172 |
D | GLY173 |
D | SER174 |
D | MET175 |
D | ILE217 |
D | SER219 |
D | ILE238 |
D | LEU242 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PXO D 355 |
Chain | Residue |
D | SER219 |
D | LEU318 |
D | TYR319 |
D | HIS320 |
D | HEM354 |
D | HOH398 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 356 |
Chain | Residue |
A | HOH430 |
A | HOH532 |
D | HOH379 |
D | HOH426 |
D | HOH452 |
D | HOH471 |
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 |