Structure of PDB 2hor Chain A

Receptor sequence

>2horA (length=425) Species: 4682 (Allium sativum)

KMTWTMKAAEEAEAVANINCSEHGRAFLDGIISEGSPKCECNTCYTGPDC
SEKIQGCSADVASGDGLFLEEYWKQHKEASAVLVSPWHRMSYFFNPVSNF
ISFELEKTIKELHEVVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTAT
PDAPESKVVAHAPFYPVFREQTKYFDKKGYVWAGNAANYVNVSNPEQYIE
MVTSPNNPEGLLRHAVIKGCKSIYDMVYYWPHYTPIKYKADEDILLFTMS
KFTGHSGSRFGWALIKDESVYNNLLNYMTKNTEGTPRETQLRSLKVLKEV
VAMVKTQKGTMRDLNTFGFKKLRERWVNITALLDQSDRFSYQELPQSEYC
NYFRRMRPPSPSYAWVKCEWEEDKDCYQTFQNGRINTQNGVGFEASSRYV
RLSLIKTQDDFDQLMYYLKDMVKAK

3D structure

• PDB: 2hor Two Structures of Alliinase from Alliium sativum L.: Apo Form and Ternary Complex with Aminoacrylate Reaction Intermediate Covalently Bound to the PLP Cofactor.
• Chain: A
• Resolution: 1.6 Å

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	SO4	A	G64 K251 R401	G64 K251 R401
BS02	SO4	A	G131 V132 T133 T248 S250 R259	G131 V132 T133 T248 S250 R259
BS03	ACT	A	Y165 D225 V227	Y165 D225 V227
BS04	SO4	A	N42 T407 Q408 D409	N42 T407 Q408 D409
BS05	SO4	A	Q75 K77 E78	Q75 K77 E78

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

External links

• PDB: RCSB:2hor, PDBe:2hor, PDBj:2hor
• PDBsum: 2hor
• PubMed: 17174334
• UniProt: Q01594|ALLN1_ALLSA Alliin lyase 1