Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GIM

CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH GDP, IMP, HADACIDIN, NO3-, AND MG2+. DATA COLLECTED AT 100K (PH 6.5)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 435

Chain	Residue
A	ASP13
A	GLY40
A	GDP432
A	NO3433
A	HDA438

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE NO3 A 433

Chain	Residue
A	GLY12
A	ASP13
A	LYS16
A	ALA39
A	GLY40
A	HIS41
A	ALA223
A	GLN224
A	GDP432
A	MG435
A	HDA438
A	IMP440

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HDA A 438

Chain	Residue
A	ASP13
A	ASN38
A	GLY40
A	THR129
A	GLY298
A	ALA299
A	THR300
A	THR301
A	ARG303
A	ARG305
A	NO3433
A	MG435
A	IMP440

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE IMP A 440

Chain	Residue
A	TRP11
A	ASP13
A	ASN38
A	ALA39
A	GLY127
A	THR128
A	THR129
A	ARG143
A	GLN224
A	LEU228
A	VAL238
A	THR239
A	VAL273
A	GLY274
A	ARG303
A	NO3433
A	HDA438
A	HOH584
A	HOH587
A	HOH601
A	HOH610
A	HOH784

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP A 432

Chain	Residue
A	ASP13
A	GLU14
A	GLY15
A	LYS16
A	GLY17
A	GLY40
A	HIS41
A	THR42
A	ARG305
A	LYS331
A	ASP333
A	SER414
A	GLY416
A	PRO417
A	NO3433
A	MG435
A	HOH574
A	HOH600
A	HOH666
A	HOH705
A	HOH801

site_id	ASP
Number of Residues	3
Details	THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE.

Chain	Residue
A	ARG305
A	THR301
A	ARG303

site_id	GNS
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	IMP
Number of Residues	6
Details	THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE.

Chain	Residue
A	ASN38
A	THR129
A	ARG143
A	GLN224
A	THR239
A	VAL273

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	1
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10346917","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"description":"in other chain"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10346917","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8961938","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9000627","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10346917","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9000627","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10346917","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9000627","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9182542, 10346917, 9202000

Chain	Residue	Details
A	ASP13
A	HIS41

site_id	MCSA1
Number of Residues	5
Details	M-CSA 65

Chain	Residue	Details
A	ASP13	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
A	LYS16	electrostatic stabiliser, hydrogen bond donor
A	GLY40	metal ligand
A	HIS41	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLN224	electrostatic stabiliser, hydrogen bond donor

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