Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6YB9

Human octameric PAICS in complex with SAICAR, AMP-PNP, and magnesium

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004638	molecular_function	phosphoribosylaminoimidazole carboxylase activity
A	0004639	molecular_function	phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006177	biological_process	GMP biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0009113	biological_process	purine nucleobase biosynthetic process
A	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0016874	molecular_function	ligase activity
A	0042802	molecular_function	identical protein binding
A	0044208	biological_process	'de novo' AMP biosynthetic process
A	0045296	molecular_function	cadherin binding
A	0070062	cellular_component	extracellular exosome
A	0097294	biological_process	'de novo' XMP biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004638	molecular_function	phosphoribosylaminoimidazole carboxylase activity
B	0004639	molecular_function	phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006177	biological_process	GMP biosynthetic process
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0009113	biological_process	purine nucleobase biosynthetic process
B	0016020	cellular_component	membrane
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0016874	molecular_function	ligase activity
B	0042802	molecular_function	identical protein binding
B	0044208	biological_process	'de novo' AMP biosynthetic process
B	0045296	molecular_function	cadherin binding
B	0070062	cellular_component	extracellular exosome
B	0097294	biological_process	'de novo' XMP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue ANP A 501

Chain	Residue
A	TYR14
A	MET93
A	LYS131
A	ASP207
A	MG507
A	HOH602
A	HOH617
A	HOH658
A	HOH699
A	GLY16
A	LYS17
A	THR18
A	LYS19
A	VAL21
A	LEU33
A	PRO89
A	CYS91

site_id	AC2
Number of Residues	20
Details	binding site for residue OK8 A 502

Chain	Residue
A	LYS17
A	THR40
A	GLY42
A	GLU97
A	ARG101
A	GLY106
A	SER107
A	ASP189
A	LYS191
A	ASP212
A	SER213
A	TRP214
A	ARG215
A	LYS228
A	ARG232
A	MG508
A	HOH621
A	HOH686
A	HOH689
A	HOH694

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 503

Chain	Residue
A	LYS178
A	GLU263
A	GLY392
A	ASN395
A	HIS396
A	HOH618

site_id	AC4
Number of Residues	7
Details	binding site for residue EDO A 504

Chain	Residue
A	ILE73
A	LYS74
A	ILE164
A	ILE203
A	LEU205
A	ILE411
A	HOH680

site_id	AC5
Number of Residues	6
Details	binding site for residue EDO A 505

Chain	Residue
A	LEU378
A	SER379
A	HOH604
B	LEU366
B	ARG367
B	LEU368

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO A 506

Chain	Residue
A	GLU317
A	GLY318
A	ASP319
A	GLY320
A	HOH648
B	GLU177
B	LYS178

site_id	AC7
Number of Residues	2
Details	binding site for residue MG A 507

Chain	Residue
A	ANP501
A	HOH658

site_id	AC8
Number of Residues	3
Details	binding site for residue MG A 508

Chain	Residue
A	GLU97
A	ASP137
A	OK8502

site_id	AC9
Number of Residues	6
Details	binding site for residue EDO B 701

Chain	Residue
A	GLU177
A	LYS178
A	HOH636
B	GLU317
B	GLY318
B	GLY320

site_id	AD1
Number of Residues	17
Details	binding site for residue ANP B 702

Chain	Residue
B	TYR14
B	GLY16
B	LYS17
B	THR18
B	LYS19
B	VAL21
B	LEU33
B	PRO89
B	CYS91
B	MET93
B	LYS131
B	ASP207
B	MG705
B	HOH805
B	HOH826
B	HOH829
B	HOH890

site_id	AD2
Number of Residues	19
Details	binding site for residue OK8 B 703

Chain	Residue
B	ASP189
B	MET190
B	LYS191
B	ASP212
B	TRP214
B	ARG215
B	LYS228
B	ARG232
B	MG706
B	HOH853
B	HOH865
B	LYS17
B	THR40
B	GLY42
B	GLU97
B	VAL99
B	ARG101
B	GLY106
B	SER107

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO B 704

Chain	Residue
B	SER274
B	THR275
B	HOH867

site_id	AD4
Number of Residues	2
Details	binding site for residue MG B 705

Chain	Residue
B	ANP702
B	HOH826

site_id	AD5
Number of Residues	4
Details	binding site for residue MG B 706

Chain	Residue
B	GLU97
B	ASP137
B	OK8703
B	HOH925

Functional Information from PROSITE/UniProt

site_id	PS01057
Number of Residues	15
Details	SAICAR_SYNTHETASE_1 SAICAR synthetase signature 1. MIPIEwVCRriaTGS

Chain	Residue	Details
A	MET93-SER107

site_id	PS01058
Number of Residues	9
Details	SAICAR_SYNTHETASE_2 SAICAR synthetase signature 2. LVDmKIEFG

Chain	Residue	Details
A	LEU187-GLY195

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Region: {"description":"Linker","evidences":[{"source":"PubMed","id":"17224163","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2H31","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	316
Details	Region: {"description":"AIR carboxylase domain","evidences":[{"source":"PubMed","id":"17224163","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2H31","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17224163","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2H31","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9DCL9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17924679","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCL9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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