Structure of PDB 6am9 Chain D

Receptor sequence
>6am9D (length=385) Species: 186497 (Pyrococcus furiosus DSM 3638) [Search protein sequence]
MWFGEFGGQYVPETLVGPLKELEKAYKRFKDDEEFNRQLNYYLKTWAGRP
TPLYYAKRLTEKIGGAKVYLKREDLVHGGAHKTNNAIGQALLAKLMGKTR
LIAETGAGQHGVATAMAGALLGMKVDIYMGAEDVERQKMNVFRMKLLGAN
VIPVNSGSRTLKDAINEALRDWVATFEYTHYLIGSVVGPHPYPTIVRDFQ
SVIGREAKAQILEAEGQLPDVIVACVGGGSNAMGIFYPFVNDKKVKLVGV
EAGGKGLESGKHSASLNAGQVGVSHGMLSYFLQDEEGQIKPSHSIAPGLD
YPGVGPEHAYLKKIQRAEYVAVTDEEALKAFHELSRTEGIIPALESAHAV
AYAMKLAKEMSRDEIIIVNLSGRGDKDLDIVLKAS
3D structure
PDB6am9 Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble.
ChainD
Resolution2.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 0JO D H81 K82 T105 G106 A107 Q109 H110 S185 G227 G229 S230 N231 G298 E345 S371 H81 K82 T105 G106 A107 Q109 H110 S185 G227 G229 S230 N231 G298 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6am9, PDBe:6am9, PDBj:6am9
PDBsum6am9
PubMed29712420
UniProtQ8U093|TRPB1_PYRFU Tryptophan synthase beta chain 1 (Gene Name=trpB1)

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