BioLiP

Structure of PDB 2clm Chain A

Receptor sequence

>2clmA (length=251) [Search protein sequence]

ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELG
VPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLM
YANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPI
FICPPNADDDLLRQVASYGRGYTYLLSHHLIEKLKEYHAAPALQGFGISS
PEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELRSFVSAMKAAS
R

3D structure

PDB

2clm Allosteric Regulation of Substrate Channeling in Tryptophan Synthase: Modulation of the L-Serine Reaction in Stage I of the Beta-Reaction by Alpha-Site Ligands.

Chain

Resolution

1.51 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 Y175
Catalytic site (residue number reindexed from 1)	E48 D59 Y174
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	F6F	A	E49 A59 I64 L100 A129 I153 Y175 F212 G213 S235	E48 A58 I63 L99 A128 I152 Y174 F196 G197 S219	PDBbind-CN: -logKd/Ki=3.55,Kd=280uM

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

PDB	RCSB:2clm, PDBe:2clm, PDBj:2clm
PDBsum	2clm
PubMed	17559232
UniProt	P00929\|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)