Structure of PDB 2qve Chain B

Receptor sequence
>2qveB (length=526) Species: 1908 (Streptomyces globisporus) [Search protein sequence]
PVSVDGETLTVEAVRRVAEERATVDVPAESIAKAQKSREIFEGIAEQNIP
IYGVTTGYGEMIYMQVDKSKEVELQTNLVRSHSAGVGPLFAEDEARAIVA
ARLNTLAKGHSAVRPIILERLAQYLNEGITPAIPEIGSLGGDLAPLSHVA
STLIGEGYVLRDGRPVETAQVLAERGIEPLELRFKEGLALINGTSGMTGL
GSLVVGRALEQAQQAEIVTALLIEAVRGSTSPFLAEGHDIARPHEGQIDT
AANMRALMRGSGLTVEHADLRRELQKDKEAGKDVQRSEIYLQKAYSLRAI
PQVVGAVRDTLYHARHKLRIELNSANDNPLFFEGKEIFHGANFHGQPIAF
AMDFVTIALTQLGVLAERQINRVLNRHLSYGLPEFLVSGDPGLHSGFAGA
QYPATALVAENRTIGPASTQSVPSNGDNQDVVSMGLISARNARRVLSNNN
KILAVEYLAAAQAVDISGRFDGLSPAAKATYEAVRRLVPTLGVDRYMADD
IELVADALSRGEFLRAIARETDIQLR
3D structure
PDB2qve Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM
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) Y63 G70 H93 N205 Y308 R311 F356 Q442
Catalytic site (residue number reindexed from 1) Y52 G59 H82 N192 Y295 R298 F343 Q429
Enzyme Commision number 4.3.1.23: tyrosine ammonia-lyase.
5.4.3.6: tyrosine 2,3-aminomutase.
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 247 B Y308 R311 Y295 R298 PDBbind-CN: -logKd/Ki=2.32,IC50=4.8mM
BS02 247 B Y63 G70 H93 X152 L156 N205 F356 Q442 Y52 G59 H82 X141 L143 N192 F343 Q429 PDBbind-CN: -logKd/Ki=2.32,IC50=4.8mM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004397 histidine ammonia-lyase activity
GO:0016829 lyase activity
GO:0016841 ammonia-lyase activity
GO:0016853 isomerase activity
GO:0050368 L-tyrosine 2,3-aminomutase activity
GO:0052883 tyrosine ammonia-lyase activity
Biological Process
GO:0006548 L-histidine catabolic process
GO:0009403 toxin biosynthetic process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qve, PDBe:2qve, PDBj:2qve
PDBsum2qve
PubMed18078753
UniProtQ8GMG0|TAM_STRGL MIO-dependent tyrosine 2,3-aminomutase

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