Structure of PDB 1n2o Chain B

Receptor sequence
>1n2oB (length=279) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
MAIPAFHPGELNVYSAPGDVADVSRALRLTGRRVMLVPTMGALHEGHLAL
VRAAKRVPGSVVVVSIFVNPMQFPRTPDDDLAQLRAEGVEIAFTPTTAAM
YPDGLRTTVQPGPLAAELEGGPRPTHFAGVLTVVLKLLQIVRPDRVFFGE
KDYQQLVLIRQLVADFNLDVAVVGVPTVREADGLAMSSRNRYLDPAQRAA
AVALSAALTAAAHAATAGAQAALDAARAVLDAAPGVAVDYLELRDIGLGP
MPLNGSGRLLVAARLGTTRLLDNIAIEIG
3D structure
PDB1n2o Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate
ChainB
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) M40 H44 H47 D88 D89 Q92 K160 S196 S197 R198
Catalytic site (residue number reindexed from 1) M40 H44 H47 D79 D80 Q83 K151 S187 S188 R189
Enzyme Commision number 6.3.2.1: pantoate--beta-alanine ligase (AMP-forming).
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 BAL B Q72 V142 Q164 Q72 V133 Q155
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004592 pantoate-beta-alanine ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0015940 pantothenate biosynthetic process
GO:0019482 beta-alanine metabolic process
Cellular Component
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:1n2o, PDBe:1n2o, PDBj:1n2o
PDBsum1n2o
PubMed12717031
UniProtP9WIL5|PANC_MYCTU Pantothenate synthetase (Gene Name=panC)

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