Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RHY

Crystal structures of Mycobacterium tuberculosis 6-oxopurine phosphoribosyltransferase which is a potential target for drug development against this disease

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006166	biological_process	purine ribonucleoside salvage
A	0006177	biological_process	GMP biosynthetic process
A	0006178	biological_process	guanine salvage
A	0006188	biological_process	IMP biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0032263	biological_process	GMP salvage
A	0032264	biological_process	IMP salvage
A	0043101	biological_process	purine-containing compound salvage
A	0046100	biological_process	hypoxanthine metabolic process
A	0046872	molecular_function	metal ion binding
A	0052657	molecular_function	guanine phosphoribosyltransferase activity
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006166	biological_process	purine ribonucleoside salvage
B	0006177	biological_process	GMP biosynthetic process
B	0006178	biological_process	guanine salvage
B	0006188	biological_process	IMP biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0032263	biological_process	GMP salvage
B	0032264	biological_process	IMP salvage
B	0043101	biological_process	purine-containing compound salvage
B	0046100	biological_process	hypoxanthine metabolic process
B	0046872	molecular_function	metal ion binding
B	0052657	molecular_function	guanine phosphoribosyltransferase activity
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006166	biological_process	purine ribonucleoside salvage
C	0006177	biological_process	GMP biosynthetic process
C	0006178	biological_process	guanine salvage
C	0006188	biological_process	IMP biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0032263	biological_process	GMP salvage
C	0032264	biological_process	IMP salvage
C	0043101	biological_process	purine-containing compound salvage
C	0046100	biological_process	hypoxanthine metabolic process
C	0046872	molecular_function	metal ion binding
C	0052657	molecular_function	guanine phosphoribosyltransferase activity
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006166	biological_process	purine ribonucleoside salvage
D	0006177	biological_process	GMP biosynthetic process
D	0006178	biological_process	guanine salvage
D	0006188	biological_process	IMP biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0032263	biological_process	GMP salvage
D	0032264	biological_process	IMP salvage
D	0043101	biological_process	purine-containing compound salvage
D	0046100	biological_process	hypoxanthine metabolic process
D	0046872	molecular_function	metal ion binding
D	0052657	molecular_function	guanine phosphoribosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 301

Chain	Residue
A	GLU122
A	ASP123
A	HOH403
A	HOH404
A	HOH448
A	HOH455

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 302

Chain	Residue
A	HOH402
A	HOH405
A	HOH447
A	ASP182
A	3QG303
A	HOH401

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE 3QG A 303

Chain	Residue
A	LEU65
A	LYS66
A	GLY67
A	SER92
A	VAL125
A	ASP126
A	SER127
A	GLY128
A	LEU129
A	THR130
A	LYS154
A	PHE175
A	VAL176
A	LEU181
A	ASP182
A	ARG188
A	MG302
A	HOH402
A	HOH403
A	HOH404
A	HOH406
A	HOH408
A	HOH449
A	HOH450
A	HOH451

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 301

Chain	Residue
B	GLU122
B	ASP123
B	HOH402
B	HOH403
B	HOH450
B	HOH455

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 302

Chain	Residue
B	ASP182
B	3QG303
B	HOH401
B	HOH404
B	HOH405

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 3QG B 303

Chain	Residue
B	LEU65
B	LYS66
B	GLY67
B	VAL125
B	ASP126
B	SER127
B	GLY128
B	LEU129
B	THR130
B	LYS154
B	PHE175
B	VAL176
B	ASP182
B	ARG188
B	MG302
B	HOH401
B	HOH404
B	HOH431
B	HOH446
B	HOH455

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 301

Chain	Residue
C	GLU122
C	ASP123
C	HOH401
C	HOH402
C	HOH403
C	HOH446

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 302

Chain	Residue
C	ASP182
C	3QG303
C	HOH404
C	HOH405
C	HOH408
C	HOH445

site_id	AC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 3QG C 303

Chain	Residue
C	HOH409
C	LEU65
C	LYS66
C	GLY67
C	SER92
C	VAL125
C	ASP126
C	SER127
C	GLY128
C	LEU129
C	THR130
C	LYS154
C	PHE175
C	VAL176
C	ASP182
C	ARG188
C	MG302
C	HOH403
C	HOH406
C	HOH408

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 301

Chain	Residue
D	GLU122
D	ASP123
D	HOH401
D	HOH402
D	HOH403
D	HOH407

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 302

Chain	Residue
D	ASP182
D	3QG303
D	HOH406
D	HOH413
D	HOH453
D	HOH460

site_id	BC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE 3QG D 303

Chain	Residue
D	LYS66
D	GLY67
D	SER92
D	VAL124
D	ASP126
D	SER127
D	GLY128
D	LEU129
D	THR130
D	LYS154
D	ASP174
D	PHE175
D	VAL176
D	ASP182
D	ARG188
D	MG302
D	HOH404
D	HOH405
D	HOH406
D	HOH412
D	HOH435
D	HOH455

Functional Information from PROSITE/UniProt

site_id	PS00103
Number of Residues	13
Details	PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDVVDSGlT

Chain	Residue	Details
A	VAL118-THR130

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0A9M2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25915781","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RHT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KNP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25915781","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RHT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)