Structure of PDB 3zp4 Chain E

Receptor sequence
>3zp4E (length=117) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MMIRGIRGATTVERDTEEEILQKTKQLLEKIIEENHTKPEDVVQMLLSAT
PDLHAVFPAKAVRELSGWQYVPVTCMQEMDVTGGLKKCIRVMMTVQTDVP
QEQIRHVYLEKAVVLRP
3D structure
PDB3zp4 Electrostatic Transition State Stabilization Rather Than Reactant Destabilization Provides the Chemical Basis for Efficient Chorismate Mutase Catalysis.
ChainE
Resolution1.798 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) R7 R63 C75 E78 Y108 R116
Catalytic site (residue number reindexed from 1) R7 R63 C75 E78 Y107 R115
Enzyme Commision number 5.4.99.5: chorismate mutase.
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 TSA E R7 X90 L115 R7 X90 L115
Gene Ontology
Molecular Function
GO:0004106 chorismate mutase activity
GO:0016853 isomerase activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0046417 chorismate metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3zp4, PDBe:3zp4, PDBj:3zp4
PDBsum3zp4
PubMed25422475
UniProtP19080|AROH_BACSU Chorismate mutase AroH (Gene Name=aroH)

[Back to BioLiP]