Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3D54

Structure of PurLQS from Thermotoga maritima

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
B	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006189	biological_process	'de novo' IMP biosynthetic process
C	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006189	biological_process	'de novo' IMP biosynthetic process
D	0004359	molecular_function	glutaminase activity
D	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
D	0005737	cellular_component	cytoplasm
D	0006189	biological_process	'de novo' IMP biosynthetic process
E	0000287	molecular_function	magnesium ion binding
E	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006164	biological_process	purine nucleotide biosynthetic process
E	0006189	biological_process	'de novo' IMP biosynthetic process
F	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006189	biological_process	'de novo' IMP biosynthetic process
G	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006189	biological_process	'de novo' IMP biosynthetic process
H	0004359	molecular_function	glutaminase activity
H	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
H	0005737	cellular_component	cytoplasm
H	0006189	biological_process	'de novo' IMP biosynthetic process
I	0000287	molecular_function	magnesium ion binding
I	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0006164	biological_process	purine nucleotide biosynthetic process
I	0006189	biological_process	'de novo' IMP biosynthetic process
J	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0006189	biological_process	'de novo' IMP biosynthetic process
K	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0006189	biological_process	'de novo' IMP biosynthetic process
L	0004359	molecular_function	glutaminase activity
L	0004642	molecular_function	phosphoribosylformylglycinamidine synthase activity
L	0005737	cellular_component	cytoplasm
L	0006189	biological_process	'de novo' IMP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA A 3003

Chain	Residue
A	ASP94
A	ASP236

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA I 3001

Chain	Residue
I	ASP94
I	ASP236

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA E 3002

Chain	Residue
E	ASP94
E	ASP236

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP A 2004

Chain	Residue
A	GLU137
A	LEU138
A	ARG139
A	ALA366
A	PHE370
A	TYR373
A	PRO385
A	GLY386
A	GLY388
A	LYS429
A	SER548
A	THR553
A	THR555
A	HIS556
A	ASP107
A	GLY135
A	GLY136

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP I 2005

Chain	Residue
I	ASP107
I	GLY135
I	GLY136
I	GLU137
I	LEU138
I	ARG139
I	ALA366
I	PHE370
I	TYR373
I	PRO385
I	GLY386
I	GLY388
I	LYS429
I	SER548
I	THR553
I	THR555
I	HIS556

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP E 2006

Chain	Residue
E	ASP107
E	GLY135
E	GLY136
E	GLU137
E	LEU138
E	ARG139
E	ALA366
E	PHE370
E	TYR373
E	PRO385
E	GLY386
E	GLY388
E	LYS429
E	SER548
E	THR553
E	THR555
E	HIS556

Functional Information from PROSITE/UniProt

site_id	PS01023
Number of Residues	13
Details	PTR2_2 PTR2 family proton/oligopeptide symporters signature 2. TseLVAkGNLGAI

Chain	Residue	Details
A	THR246-ILE258

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00420","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17154526","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17154526","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17154526","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18597481","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00420","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17154526","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	33
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17154526","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00420","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17154526","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18597481","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	3
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18597481","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"18597481","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
D	HIS186

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

Chain	Residue	Details
H	HIS186

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

Chain	Residue	Details
L	HIS186

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
D	HIS186
D	GLU193

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
H	HIS186
H	GLU193

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
L	HIS186
L	GLU193

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