Structure of PDB 4egr Chain D

Receptor sequence
>4egrD (length=434) Species: 777 (Coxiella burnetii) [Search protein sequence]
NAMDYQTIPSQGLSGEICVPGDKSISHRAVLLAAIAEGQTQVDGFLMGAD
NLAMVSALQQMGASIQVIEDENILVVEGVGMTGLQAPPEALDCGNSGTAI
RLLSGLLAGQPFNTVLTGDSSLQRRPMKRIIDPLTLMGAKIDSTGNVPPL
KIYGNPRLTGIHYQLPMASAQVKSCLLLAGLYARGKTCITEPAPSRDHTE
RLLKHFHYTLQKQSICVSGGGKLKANDISIPGDISSAAFFIVAATITPGS
AIRLCRVGVNPTRLGVINLLKMMGADIEVTHYTEKEPTADITVRHARLKG
IDIPPDQVPLTIDEFPVLLIAAAVAQGKTVLRDAAELRVKETDRIAAMVD
GLQKLGIAAESLPDGVIIQGGTLEGGEVNSYDDHRIAMAFAVAGTLAKGP
VRIRNCDNVKTSFPNFVELANEVGMNVKGVRGRG
3D structure
PDB4egr 2.50 angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with phosphoenolpyruvate
ChainD
Resolution2.5 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) K23 S24 D50 N95 R125 D313 E341 H384 R385 T411
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 PEP D K21 G95 T96 R123 D315 E343 R346 R387 K23 G97 T98 R125 D313 E341 R344 R385
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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Cellular Component
External links
PDB RCSB:4egr, PDBe:4egr, PDBj:4egr
PDBsum4egr
PubMed
UniProtQ83E11|AROA_COXBU 3-phosphoshikimate 1-carboxyvinyltransferase (Gene Name=aroA)

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