Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3SLH

1.70 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with shikimate-3-phosphate and glyphosate

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME A 439

Chain	Residue
A	ARG253
A	CYS255
A	ASP292

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BME A 440

Chain	Residue
A	GLU14
A	CYS16

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 A 441

Chain	Residue
A	GLU338
A	LYS342
A	SKM445
A	HOH493
A	HOH511
A	HOH544
A	HOH575
A	HOH1219
A	ARG127
A	SER167
A	ALA168
A	GLN169

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 442

Chain	Residue
A	ASP117
A	SER118
A	HIS281
A	HOH607
A	HOH912
A	HOH1490

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE S3P A 443

Chain	Residue
A	LYS21
A	SER22
A	ARG26
A	THR96
A	SER167
A	ALA168
A	GLN169
A	ARG194
A	ASP315
A	LYS342
A	GPJ444
A	HOH493
A	HOH511
A	HOH544
A	HOH575
A	HOH1219

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GPJ A 444

Chain	Residue
A	LYS21
A	ASN93
A	GLY95
A	THR96
A	ARG99
A	ARG123
A	GLN169
A	ASP315
A	GLU343
A	ARG346
A	HIS386
A	ARG387
A	S3P443
A	SKM445
A	HOH485
A	HOH575
A	HOH593

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SKM A 445

Chain	Residue
A	LYS21
A	SER22
A	ARG26
A	THR96
A	ALA168
A	GLN169
A	ARG194
A	ASP315
A	LYS342
A	PO4441
A	GPJ444

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 446

Chain	Residue
A	LYS301
A	GLY302
A	GLY329
A	LYS330

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 447

Chain	Residue
A	TYR180
A	GLY220
A	HOH507
A	HOH1387

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 448

Chain	Residue
A	MET1
A	GLY431

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 449

Chain	Residue
A	ALA360
A	GLU362

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 450

Chain	Residue
A	MET273
A	ARG299

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 451

Chain	Residue
A	THR142
A	PRO147
A	GLU284

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 452

Chain	Residue
A	THR344
A	ALA348
A	TYR383
A	HOH813

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG A 453

Chain	Residue
A	GLY36
A	GLN37
A	ALA225
A	ASN226
A	ASP227
A	HOH1507

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BME B 439

Chain	Residue
C	ARG155
C	ARG182
B	GLU14
B	ARG253
B	CYS255
B	ASP292
B	HOH984

site_id	BC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 B 440

Chain	Residue
B	ARG127
B	SER167
B	ALA168
B	GLN169
B	GLU338
B	LYS342
B	SKM443
B	HOH483
B	HOH527
B	HOH529
B	HOH565
B	HOH596

site_id	BC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE S3P B 441

Chain	Residue
B	LYS21
B	SER22
B	ARG26
B	THR96
B	SER167
B	ALA168
B	GLN169
B	ARG194
B	ASP315
B	LYS342
B	GPJ442
B	HOH483
B	HOH527
B	HOH529
B	HOH565
B	HOH596

site_id	CC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE GPJ B 442

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	S3P441
B	SKM443
B	HOH480
B	HOH579
B	HOH596

site_id	CC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SKM B 443

Chain	Residue
B	LYS21
B	SER22
B	ARG26
B	THR96
B	ALA168
B	GLN169
B	ARG194
B	ASP315
B	LYS342
B	PO4440
B	GPJ442

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GPJ B 444

Chain	Residue
A	ARG435
B	GLY36
B	GLN37
B	ASN226
B	ASP227

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 445

Chain	Residue
B	MET1
B	GLY431
B	ARG433

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG B 446

Chain	Residue
B	LYS210
B	ASP211
B	GLN213
B	SER214
B	ILE215

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PGE B 447

Chain	Residue
B	ARG340
B	PRO365

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 448

Chain	Residue
B	ALA348
B	TYR383
B	HOH1249

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1PE B 449

Chain	Residue
B	GLU198
B	LYS202
B	LEU208
B	ILE215
B	GLU287

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME C 439

Chain	Residue
C	GLU14
C	ARG253
C	CYS255
C	ASP292

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 440

Chain	Residue
C	PRO124
C	ARG127
C	HOH991

site_id	DC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 C 441

Chain	Residue
C	ARG127
C	SER167
C	ALA168
C	GLN169
C	GLU338
C	LYS342
C	SKM443
C	HOH502
C	HOH585
C	HOH622
C	HOH1220
C	HOH1262

site_id	DC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE GPJ C 442

Chain	Residue
C	LYS21
C	ASN93
C	GLY95
C	THR96
C	ARG123
C	GLN169
C	ASP315
C	GLU343
C	ARG346
C	HIS386
C	ARG387
C	SKM443
C	S3P444
C	HOH548
C	HOH622
C	HOH638

site_id	DC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SKM C 443

Chain	Residue
C	LYS21
C	SER22
C	ARG26
C	THR96
C	ALA168
C	GLN169
C	ARG194
C	ASP315
C	LYS342
C	PO4441
C	GPJ442
C	HOH622

site_id	DC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE S3P C 444

Chain	Residue
C	LYS21
C	SER22
C	ARG26
C	THR96
C	SER167
C	ALA168
C	GLN169
C	ARG194
C	ASP315
C	LYS342
C	GPJ442
C	HOH502
C	HOH585
C	HOH622
C	HOH1220
C	HOH1262

site_id	DC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG C 445

Chain	Residue
C	THR344
C	ALA348
C	TYR383
C	HOH1561
C	HOH1562

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 C 446

Chain	Residue
C	PRO7
C	SER8
C	GLN9
C	ASN428
C	HOH534

site_id	DC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG C 447

Chain	Residue
C	GLN4
C	ILE6
C	ASN423
C	VAL429
C	LYS430

site_id	DC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 448

Chain	Residue
C	ILE6
C	PRO7
C	LYS400

site_id	EC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 449

Chain	Residue
C	ARG253
C	ARG296
C	HOH939

site_id	EC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 C 450

Chain	Residue
C	LYS202
C	LEU208
C	LYS210

site_id	EC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME D 439

Chain	Residue
D	GLU14
D	ARG253
D	CYS255
D	ASP292

site_id	EC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 440

Chain	Residue
D	PRO124
D	ARG127
D	HOH1418

site_id	EC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE GPJ D 441

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	S3P442
D	SKM443
D	HOH516
D	HOH625
D	HOH963

site_id	EC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE S3P D 442

Chain	Residue
D	LYS21
D	SER22
D	ARG26
D	SER167
D	ALA168
D	GLN169
D	ARG194
D	ASP315
D	LYS342
D	GPJ441
D	HOH488
D	HOH554
D	HOH963
D	HOH1217
D	HOH1218

site_id	EC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SKM D 443

Chain	Residue
D	LYS21
D	SER22
D	ARG26
D	THR96
D	ALA168
D	GLN169
D	ARG194
D	ASP315
D	LYS342
D	GPJ441

site_id	EC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG D 444

Chain	Residue
A	GLY143
A	ASN144
A	HOH1320
D	SER8
D	GLN9
D	ASN428
D	HOH476

site_id	EC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG D 445

Chain	Residue
D	ASP140
D	SER141
D	THR142
D	PRO147

site_id	FC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG D 446

Chain	Residue
D	ALA348
D	TYR383

site_id	FC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 D 447

Chain	Residue
D	ARG199
D	LYS202
D	LEU208
D	LYS210

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	12
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	4
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	28
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	24
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)