Structure of PDB 5w19 Chain C

Receptor sequence
>5w19C (length=466) Species: 585 (Proteus vulgaris) [Search protein sequence]
AKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPSSAVYIDLLTD
SGTNAMSDHQWAAMITGDEAYAGSRNYYDLKDKAKELFNYDYIIPAHQGR
GAENILFPVLLKYKQKEGKAKNPVFISNFHFDTTAAHVELNGCKAINIVT
EKAFDSETYDDWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPV
SMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPKYKNATIKEVIF
DMYKYADALTMSAKKDPLLNIGGLVAIRDNEEIFTLARQRCVPMEGFVTY
GGLAGRDMAAMVQGLEEGTEEEYLHYRIGQVKYLGDRLREAGIPIQYPTG
GHAVFVDCKKLVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDPA
TGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKFATLKGLEFEY
EPPVLRHFTARLKPIE
3D structure
PDB5w19 The crystal structure of Proteus vulgaris tryptophan indole-lyase complexed with oxindolyl-L-alanine: implications for the reaction mechanism.
ChainC
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y72 F132 D133 D223 A225 K266 I391 H458
Catalytic site (residue number reindexed from 1) Y71 F131 D132 D222 A224 K265 I390 H457
Enzyme Commision number 4.1.99.1: tryptophanase.
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 9TD C T50 Q99 G100 R101 F132 D133 T134 N194 D223 R226 S263 K266 R414 T49 Q98 G99 R100 F131 D132 T133 N193 D222 R225 S262 K265 R413 MOAD: Ki~5uM
Gene Ontology
Molecular Function
GO:0009034 tryptophanase activity
GO:0016829 lyase activity
GO:0016830 carbon-carbon lyase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006568 tryptophan metabolic process
GO:0006569 tryptophan catabolic process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5w19, PDBe:5w19, PDBj:5w19
PDBsum5w19
PubMed30082510
UniProtP28796|TNAA_PROVU Tryptophanase (Gene Name=tnaA)

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