1YAS
HYDROXYNITRILE LYASE COMPLEXED WITH HISTIDINE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009694 | biological_process | jasmonic acid metabolic process |
A | 0009696 | biological_process | salicylic acid metabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0047606 | molecular_function | (S)-hydroxynitrile lyase activity |
A | 0052891 | molecular_function | aliphatic (S)-hydroxynitrile lyase activity |
A | 0052892 | molecular_function | aromatic (S)-hydroxynitrile lyase activity |
A | 0080030 | molecular_function | methyl indole-3-acetate esterase activity |
A | 0080031 | molecular_function | methyl salicylate esterase activity |
A | 0080032 | molecular_function | methyl jasmonate esterase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | THR137 |
A | ASP139 |
A | GLY140 |
A | GLY232 |
A | GLY233 |
A | LYS241 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HIS A 300 |
Chain | Residue |
A | HIS14 |
A | SER80 |
A | CYS81 |
A | TRP128 |
A | LEU148 |
A | LEU157 |
A | HIS235 |
A | LYS236 |
A | THR11 |
A | ILE12 |
site_id | CAT |
Number of Residues | 1 |
Details | BINDING SITE. |
Chain | Residue |
A | HIS235 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:14998991, ECO:0000305|PubMed:18524775 |
Chain | Residue | Details |
A | SER80 | |
A | HIS235 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10548044, ECO:0000269|PubMed:14998991, ECO:0000269|PubMed:18524775, ECO:0007744|PDB:1SCK, ECO:0007744|PDB:3C6Y, ECO:0007744|PDB:3YAS |
Chain | Residue | Details |
A | THR11 | |
A | SER80 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14998991, ECO:0007744|PDB:1SC9 |
Chain | Residue | Details |
A | LYS236 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Increases basicity of active site His => ECO:0000305|PubMed:18524775 |
Chain | Residue | Details |
A | ASP207 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1c4x |
Chain | Residue | Details |
A | ASP207 | |
A | SER80 | |
A | THR11 | |
A | HIS235 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1c4x |
Chain | Residue | Details |
A | SER80 | |
A | ASP207 | |
A | HIS235 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 217 |
Chain | Residue | Details |
A | THR11 | electrostatic stabiliser, hydrogen bond donor |
A | SER80 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
A | CYS81 | electrostatic stabiliser |
A | ASP207 | electrostatic stabiliser, increase acidity, increase basicity |
A | HIS235 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | LYS236 | activator, electrostatic stabiliser, hydrogen bond donor, steric role |