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3GDN

Almond hydroxynitrile lyase in complex with benzaldehyde

Functional Information from GO Data
ChainGOidnamespacecontents
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016829molecular_functionlyase activity
A0046593molecular_functionmandelonitrile lyase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0050898biological_processnitrile metabolic process
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0016829molecular_functionlyase activity
B0046593molecular_functionmandelonitrile lyase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0050898biological_processnitrile metabolic process
Functional Information from PROSITE/UniProt
site_idPS00623
Number of Residues24
DetailsGMC_OXRED_1 GMC oxidoreductases signature 1. GRvLGGTSiINagvYarAntsiyS
ChainResidueDetails
AGLY100-SER123

site_idPS00624
Number of Residues15
DetailsGMC_OXRED_2 GMC oxidoreductases signature 2. GTigTPqLLllSGVG
ChainResidueDetails
AGLY258-GLY272

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19256550","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11566130","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19256550","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 941
ChainResidueDetails
ACYS328electrostatic stabiliser, modifies pKa
ALYS361electrostatic stabiliser, modifies pKa
ATYR457electrostatic stabiliser, modifies pKa
AHIS459electrostatic stabiliser
ASER496electrostatic stabiliser, modifies pKa
AHIS497proton acceptor, proton donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 941
ChainResidueDetails
BCYS328electrostatic stabiliser, modifies pKa
BLYS361electrostatic stabiliser, modifies pKa
BTYR457electrostatic stabiliser, modifies pKa
BHIS459electrostatic stabiliser
BSER496electrostatic stabiliser, modifies pKa
BHIS497proton acceptor, proton donor

238895

PDB entries from 2025-07-16

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