6T7K

Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with NCP-26 and L-Proline

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004827	molecular_function	proline-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006433	biological_process	prolyl-tRNA aminoacylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue PRO A 801

Chain	Residue
A	THR359
A	TRP509
A	GLY510
A	HOH959
A	GLU361
A	ARG390
A	TRP407
A	GLU409
A	PHE454
A	THR478
A	HIS480
A	SER508

---

site_id	AC2
Number of Residues	18
Details	binding site for residue MU5 A 802

Chain	Residue
A	ARG390
A	GLU392
A	LYS394
A	GLN395
A	PHE399
A	ILE400
A	ARG401
A	THR402
A	PHE405
A	TRP407
A	GLN475
A	THR478
A	GLY510
A	THR512
A	ARG514
A	EDO818
A	HOH1007
A	HOH1027

---

site_id	AC3
Number of Residues	2
Details	binding site for residue EDO A 803

Chain	Residue
A	SER263
A	TYR746

---

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 804

Chain	Residue
A	TYR293
A	GLU296
A	HOH1029

---

site_id	AC5
Number of Residues	7
Details	binding site for residue EDO A 805

Chain	Residue
A	LYS258
A	GLU469
A	THR522
A	GLY524
A	LYS651
A	HOH911
A	HOH944

---

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO A 806

Chain	Residue
A	SER536
A	LYS537
A	TYR538
A	ILE595
A	HOH928
A	HOH1032
A	HOH1094

---

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO A 807

Chain	Residue
A	GLU305
A	LYS308
A	ARG433
A	EDO817
A	EDO822
A	HOH904

---

site_id	AC8
Number of Residues	6
Details	binding site for residue EDO A 808

Chain	Residue
A	ASN303
A	LYS307
A	VAL311
A	GLU312
A	ASN313
A	HOH901

---

site_id	AC9
Number of Residues	6
Details	binding site for residue EDO A 809

Chain	Residue
A	LYS448
A	GLU452
A	GLN475
A	THR478
A	HIS480
A	HOH959

---

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 810

Chain	Residue
A	PRO717
A	GLN720
A	ARG738
A	HOH1086

---

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO A 812

Chain	Residue
A	ARG432
A	LYS445

---

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO A 813

Chain	Residue
A	PRO337
A	TYR345
A	GLY346
A	ASP347
A	SER348
A	HOH927

---

site_id	AD4
Number of Residues	9
Details	binding site for residue EDO A 814

Chain	Residue
A	LYS527
A	GLU591
A	ARG598
A	VAL614
A	ARG615
A	ARG616
A	ASN619
A	HOH902
A	HOH1044

---

site_id	AD5
Number of Residues	4
Details	binding site for residue EDO A 815

Chain	Residue
A	THR484
A	GLN502
A	TYR503
A	HIS505

---

site_id	AD6
Number of Residues	5
Details	binding site for residue EDO A 816

Chain	Residue
A	VAL421
A	LYS422
A	PHE425
A	HOH905
A	HOH922

---

site_id	AD7
Number of Residues	5
Details	binding site for residue EDO A 817

Chain	Residue
A	LYS308
A	ARG433
A	EDO807
A	LYS304
A	GLU305

---

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO A 818

Chain	Residue
A	GLN475
A	ARG514
A	MU5802

---

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO A 819

Chain	Residue
A	ARG376
A	ARG578
A	ALA579
A	SER580

---

site_id	AE1
Number of Residues	2
Details	binding site for residue EDO A 820

Chain	Residue
A	VAL271
A	LYS272

---

site_id	AE2
Number of Residues	3
Details	binding site for residue EDO A 821

Chain	Residue
A	TYR279
A	ASP280
A	HOH963

---

site_id	AE3
Number of Residues	9
Details	binding site for residue EDO A 822

Chain	Residue
A	LEU309
A	ASP426
A	ASP429
A	LEU430
A	EDO807
A	HOH904
A	HOH919
A	HOH1011
A	HOH1050

---

site_id	AE4
Number of Residues	5
Details	binding site for residue EDO A 823

Chain	Residue
A	LEU378
A	PRO379
A	LYS415
A	GLU419
A	HOH924

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25817387","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27798837","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2014","submissionDatabase":"PDB data bank","title":"Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase)from Plasmodium falciparum in complex with Halofuginone and AMPPNP.","authors":["Dranow D.M.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4OLF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Q15","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YDQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2019","submissionDatabase":"PDB data bank","title":"Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with NCP-26 and L-Proline.","authors":["Johansson C.","Wang J.","Tye M.","Payne N.C.","Mazitschek R.","Thompson A.","Arrowsmith C.H.","Bountra C.","Edwards A.","Oppermann U.C.T."]}},{"source":"PDB","id":"6T7K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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