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BioLiP

Structure of PDB 5yhv Chain B

Receptor sequence
>5yhvB (length=387) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TDRVALRAGVPPFYVMDVWLAAAERQRTHGDLVNLSAGQPSAGAPEPVRA
AAAAALHLNQLGYSVALGIPELRDAIAADYQRRHGITVEPDAVVITTGSS
GGFLLAFLACFDAGDRVAMASPGYPCYRNILSALGCEVVEIPCGPQTRFQ
PTAQMLAEIDPPLRGVVVASPANPTGTVIPPEELAAIASWCDASDVRLIS
DEVYHGLVYQGAPQTSCAWQTSRNAVVVNSFSKYYAMTGWRLGWLLVPTV
LRRAVDCLTGNFTICPPVLSQIAAVSAFTPEATAEADGNLASYAINRSLL
LDGLRRIGIDRLAPTDGAFYVYADVSDFTSDSLAFCSKLLADTGVAIAPG
IDFDTARGGSFVRISFAGPSGDIEEALRRIGSWLPSQ
3D structure
PDB5yhv Crystal structure of an aminotransferase from Mycobacterium tuberculosis
ChainB
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.66: valine--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 PLP B Y64 I265 Y63 I264
BS02 PLP B G99 S100 S101 Y125 N174 D202 V204 Y205 S231 S233 K234 R242 G98 S99 S100 Y124 N173 D201 V203 Y204 S230 S232 K233 R241
BS03 AKG B Y81 H85 H206 T216 N230 Y80 H84 H205 T215 N229
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008483 transaminase activity
GO:0009042 valine-pyruvate transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
Cellular Component
GO:0009274 peptidoglycan-based cell wall

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5yhv, PDBe:5yhv, PDBj:5yhv
PDBsum5yhv
PubMed
UniProtP96847|AVTA_MYCTU Valine--pyruvate aminotransferase (Gene Name=aspB)

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