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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2QFS

E.coli EPSP synthase Pro101Ser liganded with S3P

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	17
Details	BINDING SITE FOR RESIDUE S3P A 701

Chain	Residue
A	LYS22
A	ASP313
A	ASN336
A	LYS340
A	FMT601
A	HOH729
A	HOH730
A	HOH740
A	HOH963
A	SER23
A	ARG27
A	THR97
A	SER169
A	SER170
A	GLN171
A	SER197
A	TYR200

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 601

Chain	Residue
A	LYS22
A	ASP313
A	GLU341
A	ARG344
A	HIS385
A	ARG386
A	S3P701

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT A 602

Chain	Residue
A	LYS22
A	ASN94
A	GLY96
A	THR97
A	ARG124
A	GLN171
A	GLU341
A	LYS411
A	HOH705

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 603

Chain	Residue
A	ALA380
A	TYR382
A	HOH779
A	HOH915
A	HOH1023

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 604

Chain	Residue
A	LYS373
A	LEU374
A	SER397
A	ASP398
A	HOH880
A	HOH1101
A	HOH1110

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 605

Chain	Residue
A	THR58
A	VAL62
A	SER63
A	TYR64
A	HOH1128
A	HOH1154

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT A 606

Chain	Residue
A	THR5
A	THR141
A	LEU143
A	ARG152
A	PHE376
A	THR402
A	HOH1015
A	HOH1066
A	HOH1210

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 607

Chain	Residue
A	THR65
A	LEU66
A	SER67
A	ARG72
A	GLU74
A	HOH939
A	HOH1286

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 608

Chain	Residue
A	ARG11
A	ASP13
A	TYR220
A	GLN425
A	HOH1196
A	HOH1222

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 609

Chain	Residue
A	LYS38
A	TYR335
A	HIS363
A	HOH1086
A	HOH1172
A	HOH1245
A	HOH1259

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 610

Chain	Residue
A	ARG298
A	GLU300
A	LEU301
A	PHE324
A	HOH991
A	HOH1279

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 611

Chain	Residue
A	ASP13
A	GLY14
A	THR259
A	HOH1185

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FMT A 612

Chain	Residue
A	HOH1198
A	HIS36
A	GLY79
A	GLY80
A	LEU182
A	SER230
A	HOH737
A	HOH888
A	HOH891
A	HOH1022

Functional Information from PROSITE/UniProt

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

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	ARG124
A	ARG344
A	ARG386
A	LYS411

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

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PDB entries from 2024-04-24

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