Structure of PDB 2ykv Chain A

Receptor sequence
>2ykvA (length=432) Species: 398267 (Mesorhizobium sp. LUK) [Search protein sequence]
ASDTAEKAQAIAAARNTFARDNPVSAGHHERARRSMPGGNTRSILFHRPF
PLVIAQGTGSRFQDVDGHAYVNFLGEYTAGLFGHSHPVIRAAVERALAVG
LNLSTQTENEALFAEAVCDRFPSIDLVRFTNSGTEANLMALATATAITGR
KTVLAFDGGYHGGLLNFASGHAPTNAPYHVVLGVYNDVEGTADLLKRHGH
DCAAILVEPMLGAGGCVPAERAFLDLLRAEASRCGALLIFDEVMTSRLSG
GGAQEMLGISADLTTLGKYIGGGMSFGAFGGRRDLMERFDPARDGAFAHA
GTFNNNILTMSAGHAALTQIYTRQAASDLSASGDRFRANLNRIAVENQAP
LQFTGLGSLGTIHFSRAPIRSAGDVRAADQQLKELFFFHMLRKGIYLAPR
GMYALSLEIADAGRDAFAEALADFIGEQRALL
3D structure
PDB2ykv Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N52 Y172 E220 D253 M256 K280 A416
Catalytic site (residue number reindexed from 1) N40 Y160 E208 D241 M244 K268 A404
Enzyme Commision number ?
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 IK2 A R54 S144 G145 T146 Y172 H173 E220 D253 V255 M256 K280 R42 S132 G133 T134 Y160 H161 E208 D241 V243 M244 K268
BS02 IK2 A A312 G313 T314 A300 G301 T302
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding

View graph for
Molecular Function
External links
PDB RCSB:2ykv, PDBe:2ykv, PDBj:2ykv
PDBsum2ykv
PubMed22745123
UniProtA3EYF7

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