Structure of PDB 1kfl Chain G

Receptor sequence
>1kflG (length=350) Species: 562 (Escherichia coli) [Search protein sequence]
MNYQNDDLRIKEIKELLPPVALLEKFPATENAANTVAHARKAIHKILKGN
DDRLLVVIGPCSIHDPVAAKEYATRLLALREELKDELEIVMRVYFEKPRT
TVGWKGLINDPHMDNSFQINDGLRIARKLLLDINDSGLPAAGEFLDMITP
QYLADLMSWGAIGARTTESQVHRELASGLSCPVGFKNGTDGTIKVAIDAI
NAAGAPHCFLSVTKWGHSAIVNTSGNGDCHIILRGGKEPNYSAKHVAEVK
EGLNKAGLPAQVMIDFSHANSSKQFKKQMDVCADVCQQIAGGEKAIIGVM
VESHLVEGNQSLESGEPLAYGKSITDACIGWEDTDALLRQLANAVKARRG
3D structure
PDB1kfl Allosteric inhibition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase alters the coordination of both substrates.
ChainG
Resolution2.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.5.1.54: 3-deoxy-7-phosphoheptulonate synthase.
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 MN G C61 H268 E302 D326 C61 H268 E302 D326
BS02 PHE G Q151 A154 L179 S180 F209 S211 V221 Q151 A154 L179 S180 F209 S211 V221
BS03 PEP G R92 K186 R234 H268 R92 K186 R234 H268
Gene Ontology
Molecular Function
GO:0003849 3-deoxy-7-phosphoheptulonate synthase activity
GO:0016740 transferase activity
GO:0042802 identical protein binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009058 biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009423 chorismate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1kfl, PDBe:1kfl, PDBj:1kfl
PDBsum1kfl
PubMed12126632
UniProtP0AB91|AROG_ECOLI Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (Gene Name=aroG)

[Back to BioLiP]