2PQ9

E. coli EPSPS liganded with (R)-difluoromethyl tetrahedral reaction intermediate analog

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	23
Details	BINDING SITE FOR RESIDUE GG9 A 501

Chain	Residue
A	LYS22
A	GLN171
A	SER197
A	TYR200
A	ASP313
A	ASN336
A	LYS340
A	ARG344
A	HIS385
A	ARG386
A	LYS411
A	SER23
A	HOH525
A	HOH534
A	HOH550
A	HOH646
A	ARG27
A	ASN94
A	GLY96
A	THR97
A	ARG124
A	SER169
A	SER170

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 502

Chain	Residue
A	LYS373
A	LEU374
A	SER397
A	ASP398
A	HOH603
A	HOH730
A	HOH838

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 503

Chain	Residue
A	ALA380
A	TYR382
A	HOH584
A	HOH735
A	HOH834

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 504

Chain	Residue
A	THR5
A	ARG152
A	THR402

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 505

Chain	Residue
A	THR58
A	SER63
A	TYR64
A	HOH627
A	HOH887

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 506

Chain	Residue
A	ARG298
A	LEU301
A	HOH869

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 507

Chain	Residue
A	THR65
A	LEU66
A	SER67
A	ARG72
A	HOH786
A	HOH913

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 508

Chain	Residue
A	ASP13
A	GLY14
A	THR259
A	HOH954

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT A 509

Chain	Residue
A	PRO199
A	HOH561

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 510

Chain	Residue
A	LYS38
A	TYR335
A	HIS363
A	HOH848

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 511

Chain	Residue
A	ARG134
A	LEU135
A	HOH695
A	HOH910

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 512

Chain	Residue
A	PRO19
A	PHE413
A	PRO414
A	ASP415
A	HOH635
A	HOH645
A	HOH732

---

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 513

Chain	Residue
A	THR263
A	GLY264
A	HOH549

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 514

Chain	Residue
A	GLU358
A	GLU360
A	ARG367
A	THR369
A	HOH654

---

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 515

Chain	Residue
A	HIS52
A	ASN94
A	GLU118
A	HOH558
A	HOH847

---

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	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	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

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