Structure of PDB 6mls Chain A

Receptor sequence
>6mlsA (length=455) Species: 546 (Citrobacter freundii) [Search protein sequence]
NYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDS
GTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRG
AENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLN
IAFKGDIDLKKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVR
ELTAAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGC
TMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEA
MAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARR
FCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLE
TVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTA
RFDYI
3D structure
PDB6mls Pressure and Temperature Effects on the Formation of Aminoacrylate Intermediates of Tyrosine Phenol-lyase Demonstrate Reaction Dynamics
ChainA
Resolution1.77 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 CQG A Q228 R323 Q227 R322
BS02 CQG A R100 F123 T124 M379 R381 F448 F449 R99 F122 T123 M378 R380 F447 F448
BS03 0JO A T49 Q98 G99 R100 F123 N185 D214 R217 S254 K257 R404 T48 Q97 G98 R99 F122 N184 D213 R216 S253 K256 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

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Molecular Function
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Biological Process
External links
PDB RCSB:6mls, PDBe:6mls, PDBj:6mls
PDBsum6mls
PubMed
UniProtP31013|TPL_CITFR Tyrosine phenol-lyase (Gene Name=tpl)

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