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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ROI

2.20 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 439

Chain	Residue
A	MET45
A	ASN70
A	PHE415
A	PRO416
A	ASN417

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 440

Chain	Residue
A	THR96
A	ARG123
A	LYS21
A	ASN93
A	SER94
A	GLY95

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 441

Chain	Residue
A	ARG406
A	ASN407

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 442

Chain	Residue
A	THR262
A	ARG263
A	LEU264
A	GLN309
A	LEU312
A	HOH566
B	LYS271

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 443

Chain	Residue
A	GLY143
B	LYS330

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 444

Chain	Residue
A	HIS160
A	GLY183
A	LYS184
A	HOH489
B	LYS222
B	LYS224

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 445

Chain	Residue
A	LYS356
A	ASN381
A	ARG406
B	GLN58

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 446

Chain	Residue
A	ARG99
A	ARG123
A	ARG127

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 447

Chain	Residue
A	SER22
A	ARG26
A	THR96
A	GLN169
A	HOH520

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 448

Chain	Residue
A	GLY329
A	LYS330
A	GLN371
A	HOH567

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 449

Chain	Residue
A	HIS297
A	ARG299
A	HOH561
A	HOH572
B	ARG299

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 450

Chain	Residue
A	ASP68
A	PRO124
A	LYS126
A	ARG127

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL B 439

Chain	Residue
B	MET45
B	ASN70
B	PHE415
B	PRO416
B	ASN417

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 440

Chain	Residue
B	SER172
B	ARG194
B	HIS196
B	THR197

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 441

Chain	Residue
B	SER167
B	ALA168

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 442

Chain	Residue
A	LYS271
B	THR262
B	ARG263
B	LEU264
B	GLN309

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 443

Chain	Residue
B	SER22
B	ARG26
B	THR96
B	ARG99
B	GLN169
B	ARG194
B	HOH505

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 444

Chain	Residue
A	LYS222
B	LYS184

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 445

Chain	Residue
B	ARG99
B	ARG123
B	GLN169

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 446

Chain	Residue
B	ASN93
B	SER94
B	GLY95
B	THR96
B	ARG99
B	ARG123
B	HOH452

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	6
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	2
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	14
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	12
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

246704

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