Structure of PDB 3slh Chain B

Receptor sequence
>3slhB (length=439) Species: 227377 (Coxiella burnetii RSA 493) [Search protein sequence]
AMDYQTIPSQGLSGEICVPGDKSISHRAVLLAAIAEGQTQVDGFLMGADN
LAMVSALQQMGASIQVIEDENILVVEGVGMTGLQAPPEALDCGNSGTAIR
LLSGLLAGQPFNTVLTGDSSLQRRPMKRIIDPLTLMGAKIDSTGNVPPLK
IYGNPRLTGIHYQLPMASAQVKSCLLLAGLYARGKTCITEPAPSRDHTER
LLKHFHYTLQKDKQSICVSGGGKLKANDISIPGDISSAAFFIVAATITPG
SAIRLCRVGVNPTRLGVINLLKMMGADIEVTHYTEKNEEPTADITVRHAR
LKGIDIPPDQVPLTIDEFPVLLIAAAVAQGKTVLRDAAELRVKETDRIAA
MVDGLQKLGIAAESLPDGVIIQGGTLEGGEVNSYDDHRIAMAFAVAGTLA
KGPVRIRNCDNVKTSFPNFVELANEVGMNVKGVRGRGGF
3D structure
PDB3slh 1.70 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase(AroA) from Coxiella burnetii in complex with shikimate-3-phosphate and glyphosate
ChainB
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) K21 S22 D48 N93 R123 D315 E343 H386 R387 T413
Catalytic site (residue number reindexed from 1) K22 S23 D49 N94 R124 D316 E344 H387 R388 T414
Enzyme Commision number 2.5.1.19: 3-phosphoshikimate 1-carboxyvinyltransferase.
Interaction with ligand
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

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Molecular Function

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Cellular Component
External links
PDB RCSB:3slh, PDBe:3slh, PDBj:3slh
PDBsum3slh
PubMed
UniProtQ83E11|AROA_COXBU 3-phosphoshikimate 1-carboxyvinyltransferase (Gene Name=aroA)

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