Structure of PDB 1a3x Chain B

Receptor sequence

>1a3xB (length=487) Species: 4932 (Saccharomyces cerevisiae)

MSRLERLTSLNVVAGSDLRRTSIIGTIGPKTNNPETLVALRKAGLNIVRM
NFSHGSYEYHKSVIDNARKSEELYPGRPLAIALDTKGPEIRTGTTTNDVD
YPIPPNHEMIFTTDDKYAKACDDKIMYVDYKNITKVISAGRIIYVDDGVL
SFQVLEVVDDKTLKVKALNAGKICSHKGVNLPGTDVDLPALSEKDKEDLR
FGVKNGVHMVFASFIRTANDVLTIREVLGEQGKDVKIIVKIENQQGVNNF
DEILKVTDGVMVARGDLGIEIPAPEVLAVQKKLIAKSNLAGKPVICATQM
LESMTYNPRPTRAEVSDVGNAILDGADCVMLSGETAKGNYPINAVTTMAE
TAVIAEQAIAYLPNYDDMRNCTPKPTSTTETVAASAVAAVFEQKAKAIIV
LSTSGTTPRLVSKYRPNCPIILVTRCPRAARFSHLYRGVFPFVFEKETDD
VEARINFGIEKAKEFGILKKGDTYVSIQGNTLQVSTV

3D structure

• PDB: 1a3x The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate.
• Chain: B
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R49 R91 K240 T298
• Catalytic site (residue number reindexed from 1): R49 R91 K240 T298
• Enzyme Commision number: 2.7.1.40: pyruvate kinase.

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	PGA	B	K240 A263 R264 G265 D266 T298	K240 A263 R264 G265 D266 T298
BS02	MN	B	F214 E242 D266	F214 E242 D266

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0004743 pyruvate kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0030955 potassium ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006090 pyruvate metabolic process
• GO:0006096 glycolytic process
• GO:0016310 phosphorylation
• GO:0032787 monocarboxylic acid metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005886 plasma membrane

External links

• PDB: RCSB:1a3x, PDBe:1a3x, PDBj:1a3x
• PDBsum: 1a3x
• PubMed: 9519410
• UniProt: P00549|KPYK1_YEAST Pyruvate kinase 1 (Gene Name=CDC19)