Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GPM

ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003921	molecular_function	GMP synthase activity
A	0003922	molecular_function	GMP synthase (glutamine-hydrolyzing) activity
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006177	biological_process	GMP biosynthetic process
A	0016874	molecular_function	ligase activity
A	0042802	molecular_function	identical protein binding
A	0046037	biological_process	GMP metabolic process
B	0000166	molecular_function	nucleotide binding
B	0003921	molecular_function	GMP synthase activity
B	0003922	molecular_function	GMP synthase (glutamine-hydrolyzing) activity
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006177	biological_process	GMP biosynthetic process
B	0016874	molecular_function	ligase activity
B	0042802	molecular_function	identical protein binding
B	0046037	biological_process	GMP metabolic process
C	0000166	molecular_function	nucleotide binding
C	0003921	molecular_function	GMP synthase activity
C	0003922	molecular_function	GMP synthase (glutamine-hydrolyzing) activity
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0006177	biological_process	GMP biosynthetic process
C	0016874	molecular_function	ligase activity
C	0042802	molecular_function	identical protein binding
C	0046037	biological_process	GMP metabolic process
D	0000166	molecular_function	nucleotide binding
D	0003921	molecular_function	GMP synthase activity
D	0003922	molecular_function	GMP synthase (glutamine-hydrolyzing) activity
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0006177	biological_process	GMP biosynthetic process
D	0016874	molecular_function	ligase activity
D	0042802	molecular_function	identical protein binding
D	0046037	biological_process	GMP metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 528

Chain	Residue
A	LYS517
A	THR521
A	ILE522
A	GLU523
A	HOH732

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 528

Chain	Residue
B	LYS517
B	THR521
B	ILE522
B	GLU523

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 530

Chain	Residue
B	POP526
B	AMP527
B	HOH609

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 528

Chain	Residue
C	LYS517
C	THR521
C	ILE522
C	GLU523

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 530

Chain	Residue
C	POP526
C	AMP527
C	HOH712

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 528

Chain	Residue
D	LYS517
D	THR521
D	ILE522
D	GLU523

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 530

Chain	Residue
D	POP526
D	AMP527

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE POP A 526

Chain	Residue
A	SER235
A	GLY237
A	VAL238
A	ASP239
A	SER240
A	LYS381
A	AMP527
A	HOH538

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP A 527

Chain	Residue
A	GLY233
A	LEU234
A	SER235
A	VAL258
A	VAL260
A	PHE315
A	POP526
A	HOH622

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIT A 529

Chain	Residue
A	SER17
A	GLN18
A	GLY58
A	GLY59
A	PRO60
A	CYS86
A	TYR87
A	SER142
A	HIS181
A	HOH653

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POP B 526

Chain	Residue
B	SER235
B	GLY237
B	VAL238
B	ASP239
B	SER240
B	LYS381
B	AMP527
B	MG530
B	HOH557
B	HOH609

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE AMP B 527

Chain	Residue
B	GLY233
B	LEU234
B	SER235
B	SER240
B	VAL258
B	VAL260
B	PHE315
B	POP526
B	MG530
B	HOH609
B	HOH635

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT B 529

Chain	Residue
B	SER17
B	GLN18
B	GLY58
B	GLY59
B	PRO60
B	CYS86
B	TYR87
B	SER142
B	HIS181

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE POP C 526

Chain	Residue
C	AMP527
C	MG530
C	HOH712
C	SER235
C	GLY237
C	VAL238
C	ASP239
C	SER240
C	LYS381

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AMP C 527

Chain	Residue
C	GLY233
C	LEU234
C	SER235
C	SER240
C	VAL258
C	VAL260
C	PHE315
C	POP526
C	MG530
C	HOH569
C	HOH637
C	HOH660

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT C 529

Chain	Residue
C	SER17
C	GLN18
C	GLY58
C	GLY59
C	PRO60
C	CYS86
C	TYR87
C	SER142
C	HIS181

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POP D 526

Chain	Residue
D	SER235
D	GLY237
D	VAL238
D	ASP239
D	SER240
D	LYS381
D	AMP527
D	MG530
D	HOH646
D	HOH668

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AMP D 527

Chain	Residue
D	GLY233
D	LEU234
D	SER235
D	VAL258
D	VAL260
D	PHE315
D	GLY405
D	POP526
D	MG530
D	HOH667

site_id	CC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIT D 529

Chain	Residue
D	SER17
D	GLN18
D	GLY58
D	GLY59
D	PRO60
D	CYS86
D	TYR87
D	PHE108
D	SER142
D	HIS181

site_id	GAA
Number of Residues	3
Details	G-TYPE GLUTAMINE AMIDOTRANSFERASE ACTIVE SITE. THESE RESIDUES ARE ARRANGED IN A CATALYTIC TRIAD SIMILAR TO THOSE FOUND IN OTHER HYDROLYTIC ENZYMES

Chain	Residue
A	CYS86
A	HIS181
A	GLU183

site_id	GBA
Number of Residues	3
Details	G-TYPE GLUTAMINE AMIDOTRANSFERASE ACTIVE SITE. THESE RESIDUES ARE ARRANGED IN A CATALYTIC TRIAD SIMILAR TO THOSE FOUND IN OTHER HYDROLYTIC ENZYMES

Chain	Residue
B	CYS86
B	HIS181
B	GLU183

site_id	GCA
Number of Residues	3
Details	G-TYPE GLUTAMINE AMIDOTRANSFERASE ACTIVE SITE. THESE RESIDUES ARE ARRANGED IN A CATALYTIC TRIAD SIMILAR TO THOSE FOUND IN OTHER HYDROLYTIC ENZYMES

Chain	Residue
C	CYS86
C	HIS181
C	GLU183

site_id	GDA
Number of Residues	3
Details	G-TYPE GLUTAMINE AMIDOTRANSFERASE ACTIVE SITE. THESE RESIDUES ARE ARRANGED IN A CATALYTIC TRIAD SIMILAR TO THOSE FOUND IN OTHER HYDROLYTIC ENZYMES

Chain	Residue
D	CYS86
D	HIS181
D	GLU183

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	792
Details	Domain: {"description":"Glutamine amidotransferase type-1"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Active site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 234

Chain	Residue	Details
A	GLY59	electrostatic stabiliser, hydrogen bond donor
A	CYS86	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	TYR87	electrostatic stabiliser, hydrogen bond donor
A	HIS181	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU183	hydrogen bond acceptor, increase acidity, increase basicity
A	ASP239	electrostatic stabiliser, hydrogen bond acceptor, metal ligand, steric role
A	LYS381	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	7
Details	M-CSA 234

Chain	Residue	Details
B	GLY59	electrostatic stabiliser, hydrogen bond donor
B	CYS86	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	TYR87	electrostatic stabiliser, hydrogen bond donor
B	HIS181	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLU183	hydrogen bond acceptor, increase acidity, increase basicity
B	ASP239	electrostatic stabiliser, hydrogen bond acceptor, metal ligand, steric role
B	LYS381	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	7
Details	M-CSA 234

Chain	Residue	Details
C	GLY59	electrostatic stabiliser, hydrogen bond donor
C	CYS86	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
C	TYR87	electrostatic stabiliser, hydrogen bond donor
C	HIS181	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLU183	hydrogen bond acceptor, increase acidity, increase basicity
C	ASP239	electrostatic stabiliser, hydrogen bond acceptor, metal ligand, steric role
C	LYS381	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	7
Details	M-CSA 234

Chain	Residue	Details
D	GLY59	electrostatic stabiliser, hydrogen bond donor
D	CYS86	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
D	TYR87	electrostatic stabiliser, hydrogen bond donor
D	HIS181	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLU183	hydrogen bond acceptor, increase acidity, increase basicity
D	ASP239	electrostatic stabiliser, hydrogen bond acceptor, metal ligand, steric role
D	LYS381	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)