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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1G6T

STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003855	molecular_function	3-dehydroquinate dehydratase activity
A	0003866	molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity
A	0004764	molecular_function	shikimate 3-dehydrogenase (NADP+) activity
A	0004765	molecular_function	shikimate kinase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 A 801

Chain	Residue
A	LYS22
A	FMT701
A	HOH805
A	HOH806
A	ASN94
A	GLY96
A	THR97
A	ARG124
A	GLN171
A	GLU341
A	LYS411
A	S3P601

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE S3P A 601

Chain	Residue
A	LYS22
A	SER23
A	ARG27
A	THR97
A	SER169
A	SER170
A	GLN171
A	SER197
A	TYR200
A	ASP313
A	ASN336
A	LYS340
A	FMT701
A	PO4801
A	HOH802
A	HOH803
A	HOH804

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT A 701

Chain	Residue
A	LYS22
A	ASP313
A	GLU341
A	ARG344
A	HIS385
A	ARG386
A	S3P601
A	PO4801

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 702

Chain	Residue
A	GLU89
A	PHE91
A	HOH883
A	HOH1154

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 703

Chain	Residue
A	THR58
A	VAL62
A	SER63
A	TYR64
A	HOH1202
A	HOH1295
A	HOH1329

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 704

Chain	Residue
A	TYR382
A	HOH919
A	HOH988
A	HOH1172

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 705

Chain	Residue
A	THR65
A	LEU66
A	SER67
A	ARG72
A	HOH1176
A	HOH1297
A	HOH1323

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 706

Chain	Residue
A	LYS373
A	LEU374
A	SER397
A	ASP398
A	HOH1003
A	HOH1122

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 707

Chain	Residue
A	PRO8
A	ILE9
A	ALA10
A	GLN425
A	ALA426
A	HOH1246

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 708

Chain	Residue
A	ASP13
A	GLY14
A	THR259
A	HOH1321
A	HOH1328

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 709

Chain	Residue
A	THR5
A	LEU143
A	ARG152
A	PHE376
A	THR402
A	HOH1031
A	HOH1308

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 710

Chain	Residue
A	ARG11
A	ASN217
A	HIS219
A	HOH1215

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 711

Chain	Residue
A	LYS38
A	TYR335
A	HIS363
A	HOH1179
A	HOH1335

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 712

Chain	Residue
A	THR263
A	ASP292
A	HOH1230

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 713

Chain	Residue
A	LEU301
A	PHE324
A	HOH1160
A	HOH1187

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU90-ALA104

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

Chain	Residue	Details
A	ARG338-GLY356

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00210, ECO:0000269\|PubMed:11171958, ECO:0000269\|PubMed:12430021, ECO:0000269\|PubMed:15736934, ECO:0000269\|PubMed:16225867, ECO:0000269\|PubMed:17855366, ECO:0000269\|PubMed:17958399, ECO:0000269\|PubMed:19211556

Chain	Residue	Details
A	ASP313

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_00210, ECO:0000269\|PubMed:15736934, ECO:0000305\|PubMed:11171958

Chain	Residue	Details
A	GLU341

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00210, ECO:0000269\|PubMed:11171958, ECO:0000269\|PubMed:12430021, ECO:0000269\|PubMed:13129913, ECO:0000269\|PubMed:15736934, ECO:0000269\|PubMed:16225867, ECO:0000269\|PubMed:17855366, ECO:0000269\|PubMed:17958399, ECO:0000269\|PubMed:19211556

Chain	Residue	Details
A	LYS22
A	SER169
A	LYS340

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00210, ECO:0000269\|PubMed:11171958, ECO:0000269\|PubMed:12430021, ECO:0000269\|PubMed:13129913, ECO:0000269\|PubMed:15736934, ECO:0000269\|PubMed:17855366, ECO:0000269\|PubMed:17958399, ECO:0000269\|PubMed:19211556

Chain	Residue	Details
A	SER197
A	ARG27
A	ASN336

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00210, ECO:0000269\|PubMed:11171958, ECO:0000269\|PubMed:16225867, ECO:0000269\|PubMed:17855366, ECO:0000269\|PubMed:19211556

Chain	Residue	Details
A	ARG344
A	ARG386
A	LYS411
A	ARG124

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Modified by bromopyruvate => ECO:0000269\|PubMed:11171958

Chain	Residue	Details
A	CYS408
A	LYS411

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 457

Chain	Residue	Details
A	ASP49	metal ligand
A	ASN94	metal ligand
A	ASP313	electrostatic stabiliser, proton shuttle (general acid/base)
A	GLU341	electrostatic stabiliser, metal ligand, proton shuttle (general acid/base)
A	HIS385	steric role
A	ARG386	transition state stabiliser
A	LYS411	steric role

218500

PDB entries from 2024-04-17

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