Structure of PDB 1lk9 Chain A

Receptor sequence
>1lk9A (length=425) Species: 4682 (Allium sativum) [Search protein sequence]
KMTWTMKAAEEAEAVANINCSEHGRAFLDGIISEGSPKCECNTCYTGPDC
SEKIQGCSADVASGDGLFLEEYWKQHKEASAVLVSPWHRMSYFFNPVSNF
ISFELEKTIKELHEVVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTAT
PDAPESKVVAHAPFYPVFREQTKYFDKKGYVWAGNAANYVNVSNPEQYIE
MVTSPNNPEGLLRHAVIKGCKSIYDMVYYWPHYTPIKYKADEDILLFTMS
KFTGHSGSRFGWALIKDESVYNNLLNYMTKNTEGTPRETQLRSLKVLKEV
VAMVKTQKGTMRDLNTFGFKKLRERWVNITALLDQSDRFSYQELPQSEYC
NYFRRMRPPSPSYAWVKCEWEEDKDCYQTFQNGRINTQNGVGFEASSRYV
RLSLIKTQDDFDQLMYYLKDMVKAK
3D structure
PDB1lk9 The active principle of garlic at atomic resolution
ChainA
Resolution1.53 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 PLP A G131 V132 T133 Y165 D225 V227 Y228 T248 S250 K251 R259 G131 V132 T133 Y165 D225 V227 Y228 T248 S250 K251 R259
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

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

[Back to BioLiP]