Structure of PDB 3ie7 Chain A

Receptor sequence
>3ie7A (length=309) Species: 1642 (Listeria innocua) [Search protein sequence]
SLIYTITLNPAIDRLLFIRGELEKRKTNRVIKTEFDCGGKGLHVSGVLSK
FGIKNEALGIAGSDNLDKLYAILKEKHINHDFLVEAGTSTRECFVVLSDD
TNGSTMIPEAGFTVSQTNKDNLLKQIAKKVKKEDMVVIAGSPPPHYTLSD
FKELLRTVKATGAFLGCDNSGEYLNLAVEMGVDFIKPNEDEVIAILDEKT
NSLEENIRTLAEKIPYLVVSLGAKGSICAHNGKLYQVIPPKVQERNDTGA
GDVFVGAFIAGLAMNMPITETLKVATGCSASKVMQQDSSSFDLEAAGKLK
NQVSIIQLE
3D structure
PDB3ie7 The crystal structure of phosphofructokinase (lin2199) from Listeria innocua in complex with ATP at 1.6A
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.144: tagatose-6-phosphate 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 ATP A N187 S219 G221 A222 G224 V241 G248 A249 G250 D251 S278 V282 N188 S220 G222 A223 G225 V242 G249 A250 G251 D252 S279 V283
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008443 phosphofructokinase activity
GO:0009024 tagatose-6-phosphate kinase activity
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005988 lactose metabolic process
GO:0016310 phosphorylation
GO:0046835 carbohydrate phosphorylation
GO:2001059 D-tagatose 6-phosphate catabolic process
Cellular Component
GO:0005829 cytosol

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Biological Process

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Cellular Component
External links
PDB RCSB:3ie7, PDBe:3ie7, PDBj:3ie7
PDBsum3ie7
PubMed
UniProtQ929S5

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