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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1G6S

STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE AND GLYPHOSATE

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	16
Details	BINDING SITE FOR RESIDUE S3P A 601

Chain	Residue
A	LYS22
A	ASP313
A	ASN336
A	LYS340
A	GPJ701
A	HOH811
A	HOH812
A	HOH813
A	SER23
A	ARG27
A	THR97
A	SER169
A	SER170
A	GLN171
A	SER197
A	TYR200

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GPJ A 701

Chain	Residue
A	LYS22
A	ASN94
A	GLY96
A	ARG124
A	GLN171
A	ASP313
A	GLU341
A	ARG344
A	HIS385
A	ARG386
A	LYS411
A	S3P601
A	HOH812
A	HOH814

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 801

Chain	Residue
A	TYR335
A	HOH986
A	HOH1030
A	HOH1074
A	HOH1365

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 802

Chain	Residue
A	THR65
A	LEU66
A	SER67
A	ARG72
A	HOH1208
A	HOH1335

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 803

Chain	Residue
A	ASP194
A	ASN333
A	HOH945
A	HOH1134
A	HOH1177

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 804

Chain	Residue
A	ALA380
A	TYR382
A	HOH926
A	HOH995
A	HOH1201

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 805

Chain	Residue
A	LYS373
A	LEU374
A	SER397
A	ASP398
A	HOH1009
A	HOH1137
A	HOH1394

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 806

Chain	Residue
A	LYS38
A	TYR335
A	HIS363
A	HOH1211
A	HOH1367

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 807

Chain	Residue
A	THR58
A	VAL62
A	SER63
A	TYR64
A	HOH1285

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 808

Chain	Residue
A	GLU89
A	LEU90
A	PHE91
A	HOH890
A	HOH1182

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 809

Chain	Residue
A	GLN145
A	TYR237
A	LEU238
A	HOH1307

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 810

Chain	Residue
A	ALA303
A	THR328
A	HOH1045

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	ARG27
A	SER197
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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