Structure of PDB 1c29 Chain A

Receptor sequence
>1c29A (length=264) [Search protein sequence]
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELG
VPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLM
YANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPI
FICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENRGPLHHLIEKLKEY
HAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLA
ELRSFVSAMKAASR
3D structure
PDB1c29 Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E49 D60 Y175
Catalytic site (residue number reindexed from 1) E48 D59 Y174
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 HE1 A F22 D60 L100 Y175 T183 G184 F212 G213 G234 S235 F21 D59 L99 Y174 T182 G183 F209 G210 G231 S232 MOAD: ic50=472nM
PDBbind-CN: -logKd/Ki=6.33,IC50=472nM
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

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Cellular Component
External links
PDB RCSB:1c29, PDBe:1c29, PDBj:1c29
PDBsum1c29
PubMed10504236
UniProtP00929|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)

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