Structure of PDB 2qfu Chain A

Receptor sequence
>2qfuA (length=427) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDV
RHMLNALTALGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMR
LLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPP
LRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPY
IDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFL
AAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGE
LNAIDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMAT
ELRKVGAEVEEGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTP
VTILDPKCTAKTFPDYFEQLARISQAA
3D structure
PDB2qfu Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) K22 S23 D49 N94 P119 R124 D313 E341 H385 R386 K411
Catalytic site (residue number reindexed from 1) K22 S23 D49 N94 P119 R124 D313 E341 H385 R386 K411
Enzyme Commision number 2.5.1.19: 3-phosphoshikimate 1-carboxyvinyltransferase.
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 GPJ A K22 G96 R124 Q171 D313 E341 R344 H385 R386 K22 G96 R124 Q171 D313 E341 R344 H385 R386 PDBbind-CN: -logKd/Ki=4.18,Ki=66uM
BS02 S3P A K22 S23 R27 T97 S169 S170 Q171 S197 Y200 D313 N336 K340 K22 S23 R27 T97 S169 S170 Q171 S197 Y200 D313 N336 K340 MOAD: Ki=66uM
BindingDB: Kd=7000nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003866 3-phosphoshikimate 1-carboxyvinyltransferase activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
Biological Process
GO:0008652 amino acid 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:2qfu, PDBe:2qfu, PDBj:2qfu
PDBsum2qfu
PubMed17855366
UniProtP0A6D3|AROA_ECOLI 3-phosphoshikimate 1-carboxyvinyltransferase (Gene Name=aroA)

[Back to BioLiP]