Structure of PDB 1lk9 Chain B

Receptor sequence
>1lk9B (length=427) Species: 4682 (Allium sativum) [Search protein sequence]
KMTWTMKAAEEAEAVANINCSEHGRAFLDGIISEGSPKCECNTCYTGPDC
SEKIQGCSADVASGDGLFLEEYWKQHKEASAVLVSPWHRMSYFFNPVSNF
ISFELEKTIKELHEVVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTAT
PDAPESKVVAHAPFYPVFREQTKYFDKKGYVWAGNAANYVNVSNPEQYIE
MVTSPNNPEGLLRHAVIKGCKSIYDMVYYWPHYTPIKYKADEDILLFTMS
KFTGHSGSRFGWALIKDESVYNNLLNYMTKNTEGTPRETQLRSLKVLKEV
VAMVKTQKGTMRDLNTFGFKKLRERWVNITALLDQSDRFSYQELPQSEYC
NYFRRMRPPSPSYAWVKCEWEEDKDCYQTFQNGRINTQNGVGFEASSRYV
RLSLIKTQDDFDQLMYYLKDMVKAKRK
3D structure
PDB1lk9 The active principle of garlic at atomic resolution
ChainB
Resolution1.53 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.4.1.4: alliin lyase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FUC B N276 K280 N276 K280
BS02 PLP B G131 V132 T133 Y165 D225 V227 Y228 T248 S250 K251 R259 G131 V132 T133 Y165 D225 V227 Y228 T248 S250 K251 R259
BS03 DHA B G64 Y165 K251 R401 G64 Y165 K251 R401
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016829 lyase activity
GO:0016846 carbon-sulfur lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0031404 chloride ion binding
GO:0042803 protein homodimerization activity
GO:0047654 alliin lyase activity
Biological Process
GO:0006520 amino acid metabolic process
Cellular Component
GO:0005773 vacuole

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lk9, PDBe:1lk9, PDBj:1lk9
PDBsum1lk9
PubMed12235163
UniProtQ01594|ALLN1_ALLSA Alliin lyase 1

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