Structure of PDB 2tpl Chain B

Receptor sequence
>2tplB (length=455) Species: 546 (Citrobacter freundii) [Search protein sequence]
NYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDS
GTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRG
AENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLN
IAFKGDIDLKKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVR
ELTAAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGC
TMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEA
MAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARR
FCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLE
TVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTA
RFDYI
3D structure
PDB2tpl The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y71 F123 T124 D214 T216 K257 R381 F448
Catalytic site (residue number reindexed from 1) Y70 F122 T123 D213 T215 K256 R380 F447
Enzyme Commision number 4.1.99.2: tyrosine phenol-lyase.
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 HPP B T49 R404 T48 R403 MOAD: Ki=1.25mM
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0016830 carbon-carbon lyase activity
GO:0050371 tyrosine phenol-lyase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006570 tyrosine metabolic process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2tpl, PDBe:2tpl, PDBj:2tpl
PDBsum2tpl
PubMed9174368
UniProtP31013|TPL_CITFR Tyrosine phenol-lyase (Gene Name=tpl)

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