Structure of PDB 5lha Chain A

Receptor sequence
>5lhaA (length=447) Species: 306 (Pseudomonas sp.) [Search protein sequence]
EKYKNAEKKFWHPMGSSAAPHRDKTLVIARGDGNYITDIDGQRMLDGVGG
LWNVNIGHNRASVKAAIAAQLDELAYYQTFDGIAHPRVFDLAERLTGMFA
QERMARVLFSSGGSDAVETALKMARQYWIASGEPGRTRFLSLRNGYHGVH
MGGTSVGGNGVYHYNHGQLLAGCHLLDTPWLYRNPWDCRDPQALTAHCIR
QLEEQIALLGAQTIAALIAEPVQGAGGVIVPPADYWPRLREVCDRHGILL
IADEVVTGFGRSGCMLGSRGWGVAPDILCLAKGITAGYIPLGATLFNQRI
ADAIENGQGFSHMIMHGYTYSGHPTACAAALAVLDIVEAEDLPGNAAKVG
AQLLEQLQPLVERYAVVGEVRGKGLMIALDLVSDKRTRQPLDPAAGQPSR
IADEARRAGVLVRPIGNKIILSPPLTLTRDEAGLMVSALEAAFARCG
3D structure
PDB5lha Explaining Operational Instability of Amine Transaminases: Substrate-Induced Inactivation Mechanism and Influence of Quaternary Structure on Enzyme-Cofactor Intermediate Stability.
ChainA
Resolution1.89 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y148 D255 K284 T321
Catalytic site (residue number reindexed from 1) Y146 D253 K282 T319
Enzyme Commision number 2.6.1.18: beta-alanine--pyruvate transaminase.
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 G115 S116 Y148 H149 G150 E222 D255 K284 G113 S114 Y146 H147 G148 E220 D253 K282
BS02 PMP A Y320 T321 Y318 T319
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016223 beta-alanine:pyruvate transaminase activity
GO:0030170 pyridoxal phosphate binding

View graph for
Molecular Function
External links
PDB RCSB:5lha, PDBe:5lha, PDBj:5lha
PDBsum5lha
PubMed
UniProtA0A1W2VMW5

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