Structure of PDB 5ghf Chain A

Receptor sequence
>5ghfA (length=431) Species: 439375 (Brucella anthropi ATCC 49188) [Search protein sequence]
QPNSLEARDIRYHLHSYTDAVRLEAEGPLVIERGDGIYVEDVSGKRYIEA
MSGLWSVGVGFSEPRLAEAAARQMKKLPFYHGPVIDLAEKLVSMAPVPMS
KAYFTNSGSEANDTVVKLIWYRSNALGEPERKKIISRKRGYHGVTIASAS
LTGLPNNHRSFDLPIDRILHTGCPHFYREGQAGESEEQFATRLADELEQL
IIAEGPHTIAAFIGEPVMGAGGVVVPPKTYWEKVQAVLKRYDILLIADEV
ICGFGRTGNLFGSQTFDMKPDILVMSKQLSSSYLPISAFLINERVYAPIA
SGHPVAAAVALENLAIIEERDLVANARDRGTYMQKRLRELQDHPLVGEVR
GVGLIAGVELVTDKQAKTGLEPTGALGAKANAVLQERGVISRAMGDTLAF
CPPLIINDQQVDTMVSALEATLNDVQASLTR
3D structure
PDB5ghf Active Site Engineering of omega-Transaminase Guided by Docking Orientation Analysis and Virtual Activity Screening
ChainA
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) Y151 E225 D258 I261 K287 A424
Catalytic site (residue number reindexed from 1) Y141 E215 D248 I251 K277 A399
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 A S117 G118 S119 Y151 H152 E225 D258 V260 I261 K287 S107 G108 S109 Y141 H142 E215 D248 V250 I251 K277
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:5ghf, PDBe:5ghf, PDBj:5ghf
PDBsum5ghf
PubMed
UniProtA6WVC6

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