Structure of PDB 4hpj Chain A

Receptor sequence
>4hpjA (length=268) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence]
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALEL
GVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLL
MYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAP
IFICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKL
KEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQ
MLAELRSFVSAMKAASRA
3D structure
PDB4hpj Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states.
ChainA
Resolution1.45 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) E49 D60 Y175
Catalytic site (residue number reindexed from 1) E49 D60 Y175
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 F9F A F22 L100 L127 A129 I153 Y175 T183 G184 F212 G213 G234 S235 F22 L100 L127 A129 I153 Y175 T183 G184 F212 G213 G234 S235
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4hpj, PDBe:4hpj, PDBj:4hpj
PDBsum4hpj
PubMed23952479
UniProtP00929|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)

[Back to BioLiP]