Structure of PDB 2q3c Chain A

Receptor sequence
>2q3cA (length=300) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
MSIAEDITQLIGRTPLVRLRRVTDGAVADIVAKLEFFNPANSVKDRIGVA
MLQAAEQAGLIKPDTIILEPTSGNTGIALAMVCAARGYRCVLTMPETMSL
ERRMLLRAYGAELILTPGADGMSGAIAKAEELAKTDQRYFVPQQFENPAN
PAIHRVTTAEEVWRDTDGKVDIVVAGVGTGGTITGVAQVIKERKPSARFV
AVEPAASPVLSGGQKGPHPIQGIGAGFVPPVLDQDLVDEIITVGNEDALN
VARRLAREEGLLVGISSGAATVAALQVARRPENAGKLIVVVLPDFGERYL
3D structure
PDB2q3c Structural Insights into Catalysis and Inhibition of O-Acetylserine Sulfhydrylase from Mycobacterium tuberculosis: CRYSTAL STRUCTURES OF THE ENZYME {alpha}-AMINOACRYLATE INTERMEDIATE AND AN ENZYME-INHIBITOR COMPLEX.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K44 S266 P293
Catalytic site (residue number reindexed from 1) K44 S266 P293
Enzyme Commision number 2.5.1.47: cysteine 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 peptide A T71 S72 G73 T75 M122 Q144 K215 G222 A225 T71 S72 G73 T75 M122 Q144 K215 G222 A225
Gene Ontology
Molecular Function
GO:0004124 cysteine synthase activity
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
GO:0030170 pyridoxal phosphate binding
GO:0080146 L-cysteine desulfhydrase activity
Biological Process
GO:0006535 cysteine biosynthetic process from serine
GO:0019344 cysteine biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2q3c, PDBe:2q3c, PDBj:2q3c
PDBsum2q3c
PubMed17567578
UniProtP9WP55|CYSK_MYCTU O-acetylserine sulfhydrylase (Gene Name=cysK1)

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