Structure of PDB 5ghg Chain B

Receptor sequence
>5ghgB (length=433) Species: 439375 (Brucella anthropi ATCC 49188) [Search protein sequence]
PNSLEARDIRYHLHSYTDAVRLEAEGPLVIERGDGIYVEDVSGKRYIEAM
SGLLSVGVGFSEPRLAEAAARQMKKLPFYHTFHGPVIDLAEKLVSMAPVP
MSKAYFTNSGSEANDTVVKLIWYRSNALGEPERKKIISRKRGYHGVTIAS
ASLTGLPNNHRSFDLPIDRILHTGCPHFYREGQAGESEEQFATRLADELE
QLIIAEGPHTIAAFIGEPVMGAGGVVVPPKTYWEKVQAVLKRYDILLIAD
EVICGFGRTGNLFGSQTFDMKPDILVMSKQLSSSYLPISAFLINERVYAP
IASGHPVAAAVALENLAIIEERDLVANARDRGTYMQKRLRELQDHPLVGE
VRGVGLIAGVELVTDKQAKTGLEPTGALGAKANAVLQERGVISRAMGDTL
AFCPPLIINDQQVDTMVSALEATLNDVQASLTR
3D structure
PDB5ghg Active Site Engineering of omega-Transaminase Guided by Docking Orientation Analysis and Virtual Activity Screening
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y20 Y151 E225 D258 I261 K287 A424
Catalytic site (residue number reindexed from 1) Y16 Y143 E217 D250 I253 K279 A401
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 PMP B S117 G118 S119 Y151 H152 E225 D258 V260 I261 K287 S109 G110 S111 Y143 H144 E217 D250 V252 I253 K279
Gene Ontology
Molecular Function
GO:0004015 adenosylmethionine-8-amino-7-oxononanoate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009102 biotin biosynthetic process
GO:0009448 gamma-aminobutyric acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5ghg, PDBe:5ghg, PDBj:5ghg
PDBsum5ghg
PubMed
UniProtA6WVC6

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