Structure of PDB 5ixj Chain B

Receptor sequence
>5ixjB (length=388) Species: 186497 (Pyrococcus furiosus DSM 3638) [Search protein sequence]
MWFGEFGGQYVPETLIEPLKELEKAYKRFKDDEEFNRQLNYYLKTWAGRP
TPLYYAKRLTEKIGGAKIYLKREDLVHGGAHKTNNAIGQALLAKFMGKTR
LIAETGAGQHGVATAMAGALLGMKVDIYMGAEDVERQKMNVFRMKLLGAN
VIPVNSGSRTLKDAINEALRDWVATFEYTHYLIGSVVGPHPYPTIVRDFQ
SVIGREAKAQILEAEGQLPDVIVACVGGGSNAMGIFYPFVNDKKVKLVGV
EAGGKGLESGKHSASLNAGQVGVFHGMLSYFLQGQIKPTHSIAPGLDYPG
VGPEHAYLKKIQRAEYVTVTDEEALKAFHELSRTEGIIPALESAHAVAYA
MKLAKEMSRDEIIIVNLSGRGDKDLDIVLKVSGNVLEH
3D structure
PDB5ixj Synthesis of beta-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase.
ChainB
Resolution1.54 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K82 E104 S371
Catalytic site (residue number reindexed from 1) K82 E104 S368
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 THR B T105 G106 A107 Q109 G298 D300 T105 G106 A107 Q109 G295 D297
Gene Ontology
Molecular Function
GO:0004834 tryptophan synthase activity
GO:0016829 lyase activity
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5ixj, PDBe:5ixj, PDBj:5ixj
PDBsum5ixj
PubMed27355405
UniProtQ8U093|TRPB1_PYRFU Tryptophan synthase beta chain 1 (Gene Name=trpB1)

[Back to BioLiP]