Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1A97

XPRTASE FROM E. COLI COMPLEXED WITH GMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0000310	molecular_function	xanthine phosphoribosyltransferase activity
A	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006166	biological_process	purine ribonucleoside salvage
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	0032265	biological_process	XMP salvage
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
A	0052657	molecular_function	guanine phosphoribosyltransferase activity
A	0097216	molecular_function	guanosine tetraphosphate binding
B	0000287	molecular_function	magnesium ion binding
B	0000310	molecular_function	xanthine phosphoribosyltransferase activity
B	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006166	biological_process	purine ribonucleoside salvage
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	0032265	biological_process	XMP salvage
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
B	0052657	molecular_function	guanine phosphoribosyltransferase activity
B	0097216	molecular_function	guanosine tetraphosphate binding
C	0000287	molecular_function	magnesium ion binding
C	0000310	molecular_function	xanthine phosphoribosyltransferase activity
C	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006166	biological_process	purine ribonucleoside salvage
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	0032265	biological_process	XMP salvage
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0051289	biological_process	protein homotetramerization
C	0052657	molecular_function	guanine phosphoribosyltransferase activity
C	0097216	molecular_function	guanosine tetraphosphate binding
D	0000287	molecular_function	magnesium ion binding
D	0000310	molecular_function	xanthine phosphoribosyltransferase activity
D	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006166	biological_process	purine ribonucleoside salvage
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	0032265	biological_process	XMP salvage
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0051289	biological_process	protein homotetramerization
D	0052657	molecular_function	guanine phosphoribosyltransferase activity
D	0097216	molecular_function	guanosine tetraphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BO3 D 301

Chain	Residue
B	ASP66
B	ASN67
D	VAL35
D	ARG37
D	GLY38
D	ASP88

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BO3 A 302

Chain	Residue
A	ASP88
C	ASN67
A	VAL35
A	SER36
A	GLY38

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BO3 C 303

Chain	Residue
C	VAL35
C	SER36
C	GLY38
C	ASP88
C	5GP306

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BO3 B 304

Chain	Residue
B	SER36
B	ARG37
B	GLY38
B	ASP88
B	5GP305

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 5GP B 305

Chain	Residue
B	ARG69
B	LEU90
B	ASP92
B	THR93
B	GLY94
B	THR96
B	TRP134
B	ILE135
B	BO3304
B	HOH401

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 5GP C 306

Chain	Residue
C	ARG69
C	ASP88
C	LEU90
C	ASP92
C	THR93
C	GLY94
C	GLY95
C	THR96
C	LYS115
C	TRP134
C	ILE135
C	BO3303
C	HOH417

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE84-THR96

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9743633","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1A95","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	23
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9743633","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A97","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9100006","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9743633","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A96","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
A	ASP92
A	ASP88
A	LYS115
A	ASP89

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
B	ASP92
B	ASP88
B	LYS115
B	ASP89

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
C	ASP92
C	ASP88
C	LYS115
C	ASP89

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
D	ASP92
D	ASP88
D	LYS115
D	ASP89

site_id	CSA5
Number of Residues	5
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
C	ASP92
C	ASP88
C	ARG119
C	LYS115
C	ASP89

site_id	CSA6
Number of Residues	5
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
D	ASP92
D	ASP88
D	ARG119
D	LYS115
D	ASP89

site_id	CSA7
Number of Residues	5
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
A	ASP92
A	ASP88
A	ARG119
A	LYS115
A	ASP89

site_id	CSA8
Number of Residues	5
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
B	ASP92
B	ASP88
B	ARG119
B	LYS115
B	ASP89

site_id	MCSA1
Number of Residues	3
Details	M-CSA 391

Chain	Residue	Details
A	ASP88	electrostatic stabiliser
A	ASP89	electrostatic stabiliser
A	ASP92	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	3
Details	M-CSA 391

Chain	Residue	Details
B	ASP88	electrostatic stabiliser
B	ASP89	electrostatic stabiliser
B	ASP92	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	3
Details	M-CSA 391

Chain	Residue	Details
C	ASP88	electrostatic stabiliser
C	ASP89	electrostatic stabiliser
C	ASP92	proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	3
Details	M-CSA 391

Chain	Residue	Details
D	ASP88	electrostatic stabiliser
D	ASP89	electrostatic stabiliser
D	ASP92	proton shuttle (general acid/base)

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