Structure of PDB 2yct Chain A

Receptor sequence

>2yctA (length=455) Species: 546 (Citrobacter freundii)

NYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDS
GTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRG
AENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLN
IAFKGDIDLKKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVR
ELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGC
TMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEA
MAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARR
FCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLE
TVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTA
RFDYI

3D structure

• PDB: 2yct Crystallographic Snapshots of Tyrosine Phenol-Lyase Show that Substrate Strain Plays a Role in C-C Bond Cleavage
• Chain: A
• Resolution: 2.25 Å

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	A	Q98 G99 R100 F123 D214 R217 S254 K257	Q97 G98 R99 F122 D213 R216 S253 K256
BS02	PLI	A	T49 S51 Q98 G99 R100 F123 N185 D214 R217 S254 K257 R404	T48 S50 Q97 G98 R99 F122 N184 D213 R216 S253 K256 R403
BS03	9PO	A	R100 F123 T124 M379 R381 F448 F449	R99 F122 T123 M378 R380 F447 F448
BS04	9PO	A	S12 W61	S11 W60
BS05	PO4	A	T49 F123 N185 R404	T48 F122 N184 R403

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

External links

• PDB: RCSB:2yct, PDBe:2yct, PDBj:2yct
• PDBsum: 2yct
• PubMed: 21899319
• UniProt: P31013|TPL_CITFR Tyrosine phenol-lyase (Gene Name=tpl)