Structure of PDB 2clf Chain B

Receptor sequence

>2clfB (length=394)

TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVRAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARG

3D structure

• PDB: 2clf Synthesis and Characterization of Allosteric Probes of Substrate Channeling in the Tryptophan Synthase Bienzyme Complex.
• Chain: B
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K87 E109 S377
• Catalytic site (residue number reindexed from 1): K86 E108 S376
• 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	B	P18 G395	P17 G394	MOAD: Kd=280uM PDBbind-CN: -logKd/Ki=3.55,Kd=280uM
BS02	F6F	B	E109 T110 G111 H115 L166 C170 L188 G189 T190 F280	E108 T109 G110 H114 L165 C169 L187 G188 T189 F279	MOAD: Kd=280uM PDBbind-CN: -logKd/Ki=3.55,Kd=280uM
BS03	PLP	B	H86 K87 T190 G232 G233 G234 S235 N236 E350 S377 G378	H85 K86 T189 G231 G232 G233 S234 N235 E349 S376 G377

Gene Ontology

Molecular Function

• GO:0004834 tryptophan synthase activity
• GO:0005515 protein binding
• GO:0016829 lyase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0000162 tryptophan biosynthetic process
• GO:0006568 tryptophan metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2clf, PDBe:2clf, PDBj:2clf
• PDBsum: 2clf
• PubMed: 17559195
• UniProt: P0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)