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8EUO

Hydroxynitrile Lyase from Hevea brasiliensis with Seven Mutations

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0009694biological_processjasmonic acid metabolic process
A0009696biological_processsalicylic acid metabolic process
A0016829molecular_functionlyase activity
A0047606molecular_function(S)-hydroxynitrile lyase activity
A0052891molecular_functionaliphatic (S)-hydroxynitrile lyase activity
A0052892molecular_functionaromatic (S)-hydroxynitrile lyase activity
A0080030molecular_functionmethyl indole-3-acetate esterase activity
A0080031molecular_functionmethyl salicylate esterase activity
A0080032molecular_functionmethyl jasmonate esterase activity
Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VILVGHSLGG
ChainResidueDetails
AVAL74-GLY83

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues236
DetailsDomain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"14998991","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18524775","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10548044","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14998991","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18524775","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3C6Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3YAS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14998991","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SC9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Increases basicity of active site His","evidences":[{"source":"PubMed","id":"18524775","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 217
ChainResidueDetails
AGLY11electrostatic stabiliser, hydrogen bond donor
ASER80electrostatic stabiliser, proton acceptor, proton donor, proton relay
ALEU81electrostatic stabiliser
AASP207electrostatic stabiliser, increase acidity, increase basicity
AHIS235hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AMET236activator, electrostatic stabiliser, hydrogen bond donor, steric role

247035

PDB entries from 2026-01-07

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