Structure of PDB 3fjz Chain A

Receptor sequence
>3fjzA (length=427) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDV
RHMLNALTALGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGIAMR
PLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPP
LRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPY
IDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFL
AAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGE
LNAIDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMAT
ELRKVGAEVEEGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTP
VTILDPKCTAKTFPDYFEQLARISQAA
3D structure
PDB3fjz Structural Basis of Glyphosate Resistance Resulting from the Double Mutation Thr97 -> Ile and Pro101 -> Ser in 5-Enolpyruvylshikimate-3-phosphate Synthase from Escherichia coli.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 SER A I265 G266 S269 I265 G266 S269
BS02 GPF A K22 G96 R124 Q171 D313 E341 R344 H385 R386 K22 G96 R124 Q171 D313 E341 R344 H385 R386 MOAD: Ki=90uM
PDBbind-CN: -logKd/Ki=4.05,Ki=90uM
BindingDB: Ki=160nM,Kd=160nM,koff=0.120000s-1,IC50=2000nM,kon=0.000001M-1-s-1
BS03 S3P A K22 S23 R27 I97 S169 S170 Q171 S197 Y200 D313 N336 K340 K22 S23 R27 I97 S169 S170 Q171 S197 Y200 D313 N336 K340 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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3fjz, PDBe:3fjz, PDBj:3fjz
PDBsum3fjz
PubMed19211556
UniProtP0A6D3|AROA_ECOLI 3-phosphoshikimate 1-carboxyvinyltransferase (Gene Name=aroA)

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