Structure of PDB 4yca Chain B

Receptor sequence
>4ycaB (length=286) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
LSVAIIGPGAVGTTIAYELQQSLPHTTLIGRHAKTITYYTVPHAPAQDIV
VKGYEDVTNTFDVIIIAVKTHQLDAVIPHLTYLAHEDTLIILAQNGYGQL
EHIPFKNVCQAVVYISGQKKGDVVTHFRDYQLRIQDNALTRQFRDLVQDS
QIDIVLEANIQQAIWYKLLVNLGINSITALGRQTVAIMHNPEIRILCRQL
LLDGCRVAQAEGLNFSEQTVDTIMTIYQGYPDEMGTSMYYDIVHQQPLEV
EAIQGFIYRRAREHNLDTPYLDTIYSFLRAYQQNEG
3D structure
PDB4yca Evidence of Kinetic Cooperativity in Dimeric Ketopantoate Reductase from Staphylococcus aureus.
ChainB
Resolution1.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K169
Catalytic site (residue number reindexed from 1) K167
Enzyme Commision number 1.1.1.169: 2-dehydropantoate 2-reductase.
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 NDP B G9 P10 G11 A12 V13 R33 Y56 V70 Q74 V78 N97 V115 I117 S118 G119 K121 E251 G7 P8 G9 A10 V11 R31 Y54 V68 Q72 V76 N95 V113 I115 S116 G117 K119 E249 MOAD: Kd=117nM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004616 phosphogluconate dehydrogenase (decarboxylating) activity
GO:0008677 2-dehydropantoate 2-reductase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0015940 pantothenate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4yca, PDBe:4yca, PDBj:4yca
PDBsum4yca
PubMed25946571
UniProtA0A0J9X283

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