3NVS

1.02 Angstrom resolution crystal structure of 3-phosphoshikimate 1-carboxyvinyltransferase from Vibrio cholerae in complex with shikimate-3-phosphate (partially photolyzed) and glyphosate

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	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 427

Chain	Residue
A	LYS22
A	ASP314
A	ASN337
A	LYS341
A	GPJ429
A	HOH503
A	HOH725
A	HOH826
A	SER23
A	ARG27
A	THR97
A	SER170
A	SER171
A	GLN172
A	SER198
A	TYR201

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SKM A 428

Chain	Residue
A	LYS22
A	SER23
A	ARG27
A	THR97
A	GLN172
A	TYR201
A	ASP314
A	LYS341
A	GPJ429
A	PO4438
A	HOH503

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GPJ A 429

Chain	Residue
A	LYS22
A	ASN94
A	GLY96
A	ARG124
A	GLN172
A	ASP314
A	GLU342
A	ARG345
A	HIS386
A	ARG387
A	LYS412
A	S3P427
A	SKM428
A	HOH604
A	HOH826

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 430

Chain	Residue
A	GLU123
A	GLN145
A	HOH753
A	HOH871
A	HOH901
A	HOH927
A	HOH1041

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 431

Chain	Residue
A	HOH608
A	HOH732
A	HOH733
A	HOH734
A	HOH735
A	HOH1102

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG A 432

Chain	Residue
A	HOH524
A	HOH533
A	HOH740
A	HOH741
A	HOH742
A	HOH743
A	HOH744
A	HOH953

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 433

Chain	Residue
A	ASP293
A	ARG354
A	VAL360

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 434

Chain	Residue
A	ASN17
A	LYS420
A	GLN423

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 435

Chain	Residue
A	ALA378
A	ALA379
A	HOH579
A	HOH971

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 436

Chain	Residue
A	ARG354
A	GLU362
A	HOH745
A	HOH866

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EPE A 437

Chain	Residue
A	LYS268
A	ASP279
A	TRP290
A	HOH738
A	HOH751
A	HOH861

---

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 438

Chain	Residue
A	SER170
A	SER171
A	VAL197
A	SER198
A	ASN337
A	LYS341
A	SKM428
A	HOH725
A	HOH826

---

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. RvKETDRLaAMateLrkVG

Chain	Residue	Details
A	ARG339-GLY357

---

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

Chain	Residue	Details
A	ASP314

---

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	GLN172
A	ARG345
A	ARG387
A	LYS412

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:3NVS

Chain	Residue	Details
A	SER23
A	ARG27
A	SER170
A	SER171
A	SER198
A	ASP314
A	ASN337
A	LYS341

---