Structure of PDB 2tpl Chain B Binding Site BS01

Receptor Information
>2tpl Chain B (length=455) Species: 546 (Citrobacter freundii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDS
GTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRG
AENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLN
IAFKGDIDLKKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVR
ELTAAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGC
TMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEA
MAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARR
FCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLE
TVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTA
RFDYI
Ligand information
Ligand IDHPP
InChIInChI=1S/C9H10O3/c10-8-4-1-7(2-5-8)3-6-9(11)12/h1-2,4-5,10H,3,6H2,(H,11,12)
InChIKeyNMHMNPHRMNGLLB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)CCc1ccc(O)cc1
OpenEye OEToolkits 1.5.0c1cc(ccc1CCC(=O)O)O
CACTVS 3.341OC(=O)CCc1ccc(O)cc1
FormulaC9 H10 O3
NameHYDROXYPHENYL PROPIONIC ACID
ChEMBLCHEMBL1172560
DrugBankDB03897
ZINCZINC000008383206
PDB chain2tpl Chain B Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		T49 R404
Binding residue
(residue number reindexed from 1)		T48 R403
Annotation score2
Binding affinityMOAD: Ki=1.25mM
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.
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

View graph for
Molecular Function
View graph for
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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