3FJX

E. coli EPSP synthase (T97I) liganded with S3P

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	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 428

Chain	Residue
A	LYS22
A	ASP313
A	ASN336
A	LYS340
A	FMT429
A	HOH462
A	HOH470
A	HOH780
A	SER23
A	ARG27
A	ILE97
A	SER169
A	SER170
A	GLN171
A	SER197
A	TYR200

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 429

Chain	Residue
A	LYS22
A	ASP313
A	GLU341
A	ARG344
A	HIS385
A	ARG386
A	S3P428

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 430

Chain	Residue
A	ALA380
A	TYR382
A	HOH511
A	HOH681
A	HOH751

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 431

Chain	Residue
A	LYS373
A	LEU374
A	SER397
A	ASP398
A	HOH589
A	HOH767
A	HOH782

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT A 432

Chain	Residue
A	LYS22
A	ASN94
A	GLY96
A	ILE97
A	ARG124
A	GLU341
A	LYS411
A	HOH588

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 433

Chain	Residue
A	TYR335
A	VAL339
A	HOH642
A	HOH660
A	HOH709

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 434

Chain	Residue
A	THR58
A	VAL62
A	SER63
A	TYR64
A	HOH748

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 435

Chain	Residue
A	THR65
A	LEU66
A	SER67
A	ARG72

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 436

Chain	Residue
A	ARG298
A	GLU300
A	LEU301
A	PHE324
A	HOH716

---

Functional Information from PROSITE/UniProt

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

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:0000305|PubMed:13129913

Chain	Residue	Details
A	ASP313

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210

Chain	Residue	Details
A	LYS22
A	GLY96
A	ARG124
A	GLN171
A	ARG344
A	ARG386
A	LYS411

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S

Chain	Residue	Details
A	SER23
A	ARG27
A	SER169
A	SER170
A	SER197
A	ASP313
A	ASN336
A	LYS340

---

site_id	SWS_FT_FI4
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	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1g6t

Chain	Residue	Details
A	LYS22
A	ASP313
A	LYS411
A	HIS385
A	GLU341

---

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

---