Structure of PDB 2yky Chain A

Receptor sequence
>2ykyA (length=431) Species: 398267 (Mesorhizobium sp. LUK) [Search protein sequence]
SDTAEKAQAIAAARNTFARDNPVSAGHHERARRSMPGGNTRSILFHRPFP
LVIAQGTGSRFQDVDGHAYVNFLGEYTAGLFGHSHPVIRAAVERALAVGL
NLSTQTENEALFAEAVCDRFPSIDLVRFTNSGTEANLMALATATAITGRK
TVLAFDGGYHGGLLNFASGHAPTNAPYHVVLGVYNDVEGTADLLKRHGHD
CAAILVEPMLGAGGCVPAERAFLDLLRAEASRCGALLIFDEVMTSRLSGG
GAQEMLGISADLTTLGKYIGGGMSFGAFGGRRDLMERFDPARDGAFAHAG
TFNNNILTMSAGHAALTQIYTRQAASDLSASGDRFRANLNRIAVENQAPL
QFTGLGSLGTIHFSRAPIRSAGDVRAADQQLKELFFFHMLRKGIYLAPRG
MYALSLEIADAGRDAFAEALADFIGEQRALL
3D structure
PDB2yky Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase.
ChainA
Resolution1.69 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) N39 Y159 E207 D240 M243 K267 A403
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 PLP A G145 T146 Y172 H173 E220 D253 V255 M256 K280 G132 T133 Y159 H160 E207 D240 V242 M243 K267
BS02 SFE A R54 I56 Y89 Y172 A225 K280 R412 R41 I43 Y76 Y159 A212 K267 R399
BS03 SFE A P221 A231 R233 L269 L368 P208 A218 R220 L256 L355
BS04 PLP A G313 T314 G300 T301
BS05 SFE A G313 T314 G300 T301
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding

View graph for
Molecular Function
External links
PDB RCSB:2yky, PDBe:2yky, PDBj:2yky
PDBsum2yky
PubMed22745123
UniProtA3EYF7

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