Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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STRUCTURE OF GUANINE NUCLEOTIDE (GPPCP) COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI AT PH 6.5 AND 25 DEGREES CELSIUS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004019	molecular_function	adenylosuccinate synthase activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006974	biological_process	DNA damage response
A	0015949	biological_process	nucleobase-containing small molecule interconversion
A	0016020	cellular_component	membrane
A	0016874	molecular_function	ligase activity
A	0044208	biological_process	'de novo' AMP biosynthetic process
A	0046040	biological_process	IMP metabolic process
A	0046086	biological_process	adenosine biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0097216	molecular_function	guanosine tetraphosphate binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0004019	molecular_function	adenylosuccinate synthase activity
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006974	biological_process	DNA damage response
B	0015949	biological_process	nucleobase-containing small molecule interconversion
B	0016020	cellular_component	membrane
B	0016874	molecular_function	ligase activity
B	0044208	biological_process	'de novo' AMP biosynthetic process
B	0046040	biological_process	IMP metabolic process
B	0046086	biological_process	adenosine biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0097216	molecular_function	guanosine tetraphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GCP A 432

Chain	Residue
A	ASP13
A	GLU14
A	GLY15
A	LYS16
A	GLY17
A	ALA39
A	GLY40
A	ALA223
A	LYS331
A	ASP333
A	PHE383
A	SER414
A	GLY416
A	PRO417
A	HOH573

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GCP B 433

Chain	Residue
B	GLY12
B	ASP13
B	GLU14
B	GLY15
B	LYS16
B	GLY17
B	LYS331
B	ASP333
B	SER414
B	GLY416
B	PRO417
B	HOH480
B	HOH539

site_id	GNA
Number of Residues	13
Details	THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE.

Chain	Residue
A	ASP13
A	SER414
A	THR415
A	GLY416
A	PRO417
A	GLU14
A	GLY15
A	LYS16
A	GLY17
A	LYS18
A	LYS331
A	LEU332
A	ASP333

site_id	GNB
Number of Residues	13
Details	THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE.

Chain	Residue
B	ASP13
B	GLU14
B	GLY15
B	LYS16
B	GLY17
B	LYS18
B	LYS331
B	LEU332
B	ASP333
B	SER414
B	THR415
B	GLY416
B	PRO417

Functional Information from PROSITE/UniProt

site_id	PS00513
Number of Residues	12
Details	ADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPaYedKvaR

Chain	Residue	Details
A	GLY132-ARG143

site_id	PS01266
Number of Residues	8
Details	ADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG

Chain	Residue	Details
A	GLN10-GLY17

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	GLU14
B	GLU14

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	THR42
B	THR42

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00011, ECO:0000269\|PubMed:10346917

Chain	Residue	Details
A	LEU332
A	THR415
B	ASP13
B	ARG306
B	LEU332
B	THR415
A	ASP13
A	ARG306

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00011, ECO:0000269\|PubMed:10346917, ECO:0000269\|PubMed:8961938, ECO:0000269\|PubMed:9000627

Chain	Residue	Details
B	GLU14
B	HIS41
A	GLU14
A	HIS41

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: in other chain

Chain	Residue	Details
A	ALA39
B	ALA39

site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_00011, ECO:0000269\|PubMed:10346917, ECO:0000269\|PubMed:9000627

Chain	Residue	Details
A	GLY130
A	GLY225
A	SER240
A	ARG304
B	GLY130
B	GLY225
B	SER240
B	ARG304

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00011, ECO:0000269\|PubMed:10346917, ECO:0000269\|PubMed:9000627

Chain	Residue	Details
A	ARG144
B	ARG144

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	THR300
B	THR300

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 65

Chain	Residue	Details
A	GLU14	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
A	GLY17	electrostatic stabiliser, hydrogen bond donor
A	HIS41	metal ligand
A	THR42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLY225	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 65

Chain	Residue	Details
B	GLU14	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
B	GLY17	electrostatic stabiliser, hydrogen bond donor
B	HIS41	metal ligand
B	THR42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLY225	electrostatic stabiliser, hydrogen bond donor

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