Structure of PDB 1a50 Chain A

Receptor sequence
>1a50A (length=260) [Search protein sequence]
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELG
VPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLM
YANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPI
FICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENHHLIEKLKEYHAAP
ALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELRS
FVSAMKAASR
3D structure
PDB1a50 Loop closure and intersubunit communication in tryptophan synthase.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E49 D60 Y102 Y173 Y175 T183 S233 G234 S235
Catalytic site (residue number reindexed from 1) E48 D59 Y101 Y172 Y174 T182 S226 G227 S228
Enzyme Commision number 4.2.1.20: tryptophan synthase.
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 FIP A F22 D60 L100 Y175 T183 F212 G213 G234 S235 F21 D59 L99 Y174 T182 F205 G206 G227 S228 MOAD: Kd=0.35uM
PDBbind-CN: -logKd/Ki=6.70,Kd=0.2uM
Gene Ontology
Molecular Function
GO:0004834 tryptophan synthase activity
GO:0005515 protein binding
GO:0016829 lyase activity
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1a50, PDBe:1a50, PDBj:1a50
PDBsum1a50
PubMed9548921
UniProtP00929|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)

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