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8SNI

Hydroxynitrile Lyase from Hevea brasiliensis with Forty Mutations

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 Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:14998991, ECO:0000305|PubMed:18524775
ChainResidueDetails
ASER80
AHIS237
BSER80
BHIS237

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: 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
ChainResidueDetails
AGLY11
ASER80
BGLY11
BSER80

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14998991, ECO:0007744|PDB:1SC9
ChainResidueDetails
AMET238
BMET238

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Increases basicity of active site His => ECO:0000305|PubMed:18524775
ChainResidueDetails
AASP209
BASP209

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
AASP209electrostatic stabiliser, increase acidity, increase basicity
AHIS237hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AMET238activator, electrostatic stabiliser, hydrogen bond donor, steric role

site_idMCSA2
Number of Residues6
DetailsM-CSA 217
ChainResidueDetails
BGLY11electrostatic stabiliser, hydrogen bond donor
BSER80electrostatic stabiliser, proton acceptor, proton donor, proton relay
BLEU81electrostatic stabiliser
BASP209electrostatic stabiliser, increase acidity, increase basicity
BHIS237hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BMET238activator, electrostatic stabiliser, hydrogen bond donor, steric role

222926

PDB entries from 2024-07-24

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