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7YAS

HYDROXYNITRILE LYASE, LOW TEMPERATURE NATIVE STRUCTURE

Functional Information from GO Data
ChainGOidnamespacecontents
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 PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
AHOH676
AHOH755
ATHR137
AASP139
AGLY140
AGLY232
AGLY233
ALYS241

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
ALYS23
ALYS170
AHOH505
AHOH538

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
ATYR116
ATRP217
ALYS229
AHOH642
AHOH775

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EPE A 350
ChainResidue
AGLY30
AHIS31
ALYS32
AHOH546
AHOH557

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 300
ChainResidue
ATHR11
AILE12
ASER80
ACYS81
ATRP128
ALEU148
ALEU157
AHIS235
AHOH500

site_idCAT
Number of Residues3
DetailsACTIVE SITE
ChainResidue
ASER80
AASP207
AHIS235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:14998991, ECO:0000305|PubMed:18524775
ChainResidueDetails
ASER80
AHIS235

site_idSWS_FT_FI2
Number of Residues2
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
ATHR11
ASER80

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14998991, ECO:0007744|PDB:1SC9
ChainResidueDetails
ALYS236

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Increases basicity of active site His => ECO:0000305|PubMed:18524775
ChainResidueDetails
AASP207

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
AASP207
ASER80
ATHR11
AHIS235

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
ASER80
AASP207
AHIS235

site_idMCSA1
Number of Residues6
DetailsM-CSA 217
ChainResidueDetails
ATHR11electrostatic stabiliser, hydrogen bond donor
ASER80electrostatic stabiliser, proton acceptor, proton donor, proton relay
ACYS81electrostatic stabiliser
AASP207electrostatic stabiliser, increase acidity, increase basicity
AHIS235hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS236activator, electrostatic stabiliser, hydrogen bond donor, steric role

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PDB entries from 2024-10-30

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