Structure of PDB 2yhk Chain B

Receptor sequence
>2yhkB (length=455) Species: 546 (Citrobacter freundii) [Search protein sequence]
NYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDS
GTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRG
AENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLN
IAFKGDIDLKKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVR
ELTEAHGIKVFYAATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGC
TMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEA
MAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARR
FCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLE
TVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTA
RFDYI
3D structure
PDB2yhk Crystal Structure of Citrobacter Freundii Asp214Ala Tyrosine Phenol-Lyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine
ChainB
Resolution1.91 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 A214 T216 K257 R381 F448
Catalytic site (residue number reindexed from 1) Y70 F122 T123 A213 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 N185 T216 S254 K257 Q97 G98 R99 F122 N184 T215 S253 K256
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:2yhk, PDBe:2yhk, PDBj:2yhk
PDBsum2yhk
PubMed
UniProtP31013|TPL_CITFR Tyrosine phenol-lyase (Gene Name=tpl)

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