Structure of PDB 3qtt Chain A

Receptor sequence
>3qttA (length=261) Species: 119856 (Francisella tularensis subsp. tularensis) [Search protein sequence]
AMIIADNIKQFHSIRNSLIKQQKIGFVPTMGALHNGHISLIKKAKSENDV
VIVSIFVNPTQFNNPNDYQTYPNQLQQDIQILASLDVDVLFNPSEKDIYP
DGNLLRIEPKLEIANILEGKSRPGHFSGMLTVVLKLLQITKPNNLYLGEK
DYQQVMLIKQLVKDFFINTKIIVCPTQRQPSGLPLSSRNKNLTSTDIEIA
NKIYEILRQDDFSNLEELTNKINSTGAKLQYIQKLNNRIFLAFYIGKVRL
IDNFLKETGPS
3D structure
PDB3qtt Crystal Structure of Pantoate-beta-alanine Ligase from Francisella tularensis Complexed with Beta-gamma ATP and Beta-alanine.
ChainA
Resolution2.599 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M32 H36 H39 Q79 D80 I83 K152 S188 S189 R190
Catalytic site (residue number reindexed from 1) M30 H34 H37 Q77 D78 I81 K150 S186 S187 R188
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 ANP A M32 H36 G38 H39 L42 G150 K152 D153 Q179 L187 S188 S189 M30 H34 G36 H37 L40 G148 K150 D151 Q177 L185 S186 S187
BS02 PRO A M32 Q63 M131 V135 Q156 M30 Q61 M129 V133 Q154
BS03 MG A M32 G33 Y73 S189 M30 G31 Y71 S187
BS04 BAL A M32 Q63 R124 D153 R190 M30 Q61 R122 D151 R188
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004592 pantoate-beta-alanine ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0009058 biosynthetic process
GO:0015940 pantothenate biosynthetic 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:3qtt, PDBe:3qtt, PDBj:3qtt
PDBsum3qtt
PubMed
UniProtQ5NF57|PANC_FRATT Pantothenate synthetase (Gene Name=panC)

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