Structure of PDB 2yct Chain B

Receptor sequence
>2yctB (length=455) Species: 546 (Citrobacter freundii) [Search protein sequence]
NYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDS
GTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRG
AENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLN
IAFKGDIDLKKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVR
ELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGC
TMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEA
MAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARR
FCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLE
TVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTA
RFDYI
3D structure
PDB2yct Crystallographic Snapshots of Tyrosine Phenol-Lyase Show that Substrate Strain Plays a Role in C-C Bond Cleavage
ChainB
Resolution2.25 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 PLP B Q98 G99 R100 F123 D214 R217 S254 K257 Q97 G98 R99 F122 D213 R216 S253 K256
BS02 9PO B A148 G149 I336 V337 D348 A147 G148 I335 V336 D347
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
View graph for
Biological Process
External links
PDB RCSB:2yct, PDBe:2yct, PDBj:2yct
PDBsum2yct
PubMed21899319
UniProtP31013|TPL_CITFR Tyrosine phenol-lyase (Gene Name=tpl)

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