Structure of PDB 5dw0 Chain A

Receptor sequence
>5dw0A (length=388) Species: 186497 (Pyrococcus furiosus DSM 3638) [Search protein sequence]
MWFGEFGGQYVPETLIEPLKELEKAYKRFKDDEEFNRQLNYYLKTWAGRP
TPLYYAKRLTEKIGGAKIYLKREDLVHGGAHKTNNAIGQALLAKFMGKTR
LIAETGAGQHGVATAMAGALLGMKVDIYMGAEDVERQKMNVFRMKLLGAN
VIPVNSGSRTLKDAINEALRDWVATFEYTHYLIGSVVGPHPYPTIVRDFQ
SVIGREAKAQILEAEGQLPDVIVACVGGGSNAMGIFYPFVNDKKVKLVGV
EAGGKGLESGKHSASLNAGQVGVFHGMLSYFLQDEEGQIKPTHSIAPGLD
YPGVGPEHAYLKKIQRAEYVTVTDEEALKAFHELSRTEGIIPALESAHAV
AYAMKLAKEMSRDEIIIVNLSGRGDKDLDIVLKVSGNV
3D structure
PDB5dw0 Directed evolution of the tryptophan synthase beta-subunit for stand-alone function recapitulates allosteric activation.
ChainA
Resolution2.01 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 S371
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 PLS A H81 K82 T105 G106 A107 Q109 H110 S185 G227 G229 S230 N231 G298 D300 E345 S371 H81 K82 T105 G106 A107 Q109 H110 S185 G227 G229 S230 N231 G298 D300 E345 S371
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:5dw0, PDBe:5dw0, PDBj:5dw0
PDBsum5dw0
PubMed26553994
UniProtQ8U093|TRPB1_PYRFU Tryptophan synthase beta chain 1 (Gene Name=trpB1)

[Back to BioLiP]