Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4EGR

2.50 angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with phosphoenolpyruvate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003866	molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0008652	biological_process	amino acid biosynthetic process
A	0009073	biological_process	aromatic amino acid family biosynthetic process
A	0009423	biological_process	chorismate biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
B	0003824	molecular_function	catalytic activity
B	0003866	molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0008652	biological_process	amino acid biosynthetic process
B	0009073	biological_process	aromatic amino acid family biosynthetic process
B	0009423	biological_process	chorismate biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
C	0003824	molecular_function	catalytic activity
C	0003866	molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0008652	biological_process	amino acid biosynthetic process
C	0009073	biological_process	aromatic amino acid family biosynthetic process
C	0009423	biological_process	chorismate biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
D	0003824	molecular_function	catalytic activity
D	0003866	molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0008652	biological_process	amino acid biosynthetic process
D	0009073	biological_process	aromatic amino acid family biosynthetic process
D	0009423	biological_process	chorismate biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
E	0003824	molecular_function	catalytic activity
E	0003866	molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity
E	0005737	cellular_component	cytoplasm
E	0008652	biological_process	amino acid biosynthetic process
E	0009073	biological_process	aromatic amino acid family biosynthetic process
E	0009423	biological_process	chorismate biosynthetic process
E	0016740	molecular_function	transferase activity
E	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
F	0003824	molecular_function	catalytic activity
F	0003866	molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity
F	0005737	cellular_component	cytoplasm
F	0008652	biological_process	amino acid biosynthetic process
F	0009073	biological_process	aromatic amino acid family biosynthetic process
F	0009423	biological_process	chorismate biosynthetic process
F	0016740	molecular_function	transferase activity
F	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PEP A 501

Chain	Residue
A	LYS21
A	HOH671
A	HOH672
A	GLY95
A	THR96
A	ARG123
A	GLN169
A	ASP315
A	GLU343
A	ARG346
A	ARG387

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 502

Chain	Residue
A	SER22
A	ARG26
A	THR96
A	ALA168
A	GLN169
A	ARG194
A	HOH665

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 503

Chain	Residue
A	PRO124
A	LYS126
A	ARG127

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 501

Chain	Residue
B	SER22
B	ARG26
B	THR96
B	ALA168
B	GLN169
B	ARG194

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 502

Chain	Residue
B	PRO124
B	LYS126
B	ARG127

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PEP B 503

Chain	Residue
B	LYS21
B	ASN93
B	GLY95
B	THR96
B	ARG123
B	GLN169
B	ASP315
B	GLU343
B	ARG346
B	HIS386
B	ARG387
B	HOH632
B	HOH676

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 501

Chain	Residue
C	SER22
C	ARG26
C	THR96
C	ALA168
C	GLN169
C	ARG194
C	HOH669

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 502

Chain	Residue
C	LYS126
C	ARG127
C	HOH663

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PEP C 503

Chain	Residue
C	LYS21
C	GLY95
C	THR96
C	ARG123
C	GLN169
C	ASP315
C	GLU343
C	ARG346
C	HIS386
C	ARG387
C	HOH653
C	HOH670

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 501

Chain	Residue
D	SER22
D	ARG26
D	THR96
D	ALA168
D	GLN169
D	ARG194

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 502

Chain	Residue
D	PRO124
D	LYS126
D	ARG127

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PEP D 503

Chain	Residue
D	LYS21
D	ASN93
D	GLY95
D	THR96
D	ARG123
D	GLN169
D	ASP315
D	GLU343
D	ARG346
D	HIS386
D	ARG387
D	HOH635
D	HOH665

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 501

Chain	Residue
E	SER22
E	ARG26
E	THR96
E	ALA168
E	GLN169
E	ARG194
E	HOH658

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 502

Chain	Residue
E	PRO124
E	LYS126
E	ARG127

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEP E 503

Chain	Residue
E	THR96
E	ARG123
E	GLN169
E	ASP315
E	GLU343
E	ARG346
E	ARG387
E	HOH644
E	LYS21
E	GLY95

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 501

Chain	Residue
F	SER22
F	ARG26
F	THR96
F	ALA168
F	GLN169
F	ARG194

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F 502

Chain	Residue
F	PRO124
F	LYS126
F	ARG127

site_id	BC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PEP F 503

Chain	Residue
F	LYS21
F	ASN93
F	GLY95
F	THR96
F	ARG123
F	GLN169
F	ASP315
F	GLU343
F	ARG346
F	HIS386
F	ARG387
F	HOH659
F	HOH660

Functional Information from PROSITE/UniProt

site_id	PS00104
Number of Residues	15
Details	EPSP_SYNTHASE_1 EPSP synthase signature 1. LDcGNSGTAIRlLsG

Chain	Residue	Details
A	LEU89-GLY103

site_id	PS00885
Number of Residues	19
Details	EPSP_SYNTHASE_2 EPSP synthase signature 2. RvKETDRIaAMvdgLqkLG

Chain	Residue	Details
A	ARG340-GLY358

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Region: {"description":"Phosphoenolpyruvate","evidences":[{"source":"HAMAP-Rule","id":"MF_00210","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2011","submissionDatabase":"PDB data bank","title":"1.70 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase(AroA) from Coxiella burnetii in complex with shikimate-3-phosphate and glyphosate.","authoringGroup":["Center for Structural Genomics of Infectious Diseases (CSGID)"],"authors":["Light S.H.","Minasov G.","Filippova E.V.","Krishna S.N.","Shuvalova L.","Papazisi L.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"2.50 angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with phosphoenolpyruvate.","authors":["Krishna S.N.","Light S.H.","Minasov G.","Shuvalova L.","Kwon K.","Anderson W.F."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"2.50 angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with phosphoenolpyruvate.","authors":["Krishna S.N.","Light S.H.","Minasov G.","Shuvalova L.","Kwon K.","Anderson W.F."]}},{"source":"PDB","id":"4EGR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2011","submissionDatabase":"PDB data bank","title":"1.70 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase(AroA) from Coxiella burnetii in complex with shikimate-3-phosphate and glyphosate.","authoringGroup":["Center for Structural Genomics of Infectious Diseases (CSGID)"],"authors":["Light S.H.","Minasov G.","Filippova E.V.","Krishna S.N.","Shuvalova L.","Papazisi L.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2015","submissionDatabase":"PDB data bank","title":"2.55 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with shikimate-3-phosphate, phosphate, and potassium.","authors":["Light S.H.","Minasov G.","Krishna S.N.","Kwon K.","Anderson W.F."]}},{"source":"PDB","id":"3SLH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZND","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)