Structure of PDB 2hox Chain D

Receptor sequence
>2hoxD (length=427) Species: 4682 (Allium sativum) [Search protein sequence]
KMTWTMKAAEEAEAVANINCSEHGRAFLDGIISEGSPKCECNTCYTGPDC
SEKIQGCSADVASGDGLFLEEYWKQHKEASAVLVSPWHRMSYFFNPVSNF
ISFELEKTIKELHEVVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTAT
PDAPESKVVAHAPFYPVFREQTKYFDKKGYVWAGNAANYVNVSNPEQYIE
MVTSPNNPEGLLRHAVIKGCKSIYDMVYYWPHYTPIKYKADEDILLFTMS
KFTGHSGSRFGWALIKDESVYNNLLNYMTKNTEGTPRETQLRSLKVLKEV
VAMVKTQKGTMRDLNTFGFKKLRERWVNITALLDQSDRFSYQELPQSEYC
NYFRRMRPPSPSYAWVKCEWEEDKDCYQTFQNGRINTQNGVGFEASSRYV
RLSLIKTQDDFDQLMYYLKDMVKAKRK
3D structure
PDB2hox Two Structures of Alliinase from Alliium sativum L.: Apo Form and Ternary Complex with Aminoacrylate Reaction Intermediate Covalently Bound to the PLP Cofactor.
ChainD
Resolution1.4 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 P1T D G64 G131 V132 T133 Y165 N207 D225 Y228 T248 S250 K251 R259 R401 G64 G131 V132 T133 Y165 N207 D225 Y228 T248 S250 K251 R259 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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Cellular Component
External links
PDB RCSB:2hox, PDBe:2hox, PDBj:2hox
PDBsum2hox
PubMed17174334
UniProtQ01594|ALLN1_ALLSA Alliin lyase 1

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