Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VD6

Human adenylosuccinate lyase in complex with its substrate N6-(1,2- Dicarboxyethyl)-AMP, and its products AMP and fumarate.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001666	biological_process	response to hypoxia
A	0003824	molecular_function	catalytic activity
A	0004018	molecular_function	N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006167	biological_process	AMP biosynthetic process
A	0006177	biological_process	GMP biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0007584	biological_process	response to nutrient
A	0009060	biological_process	aerobic respiration
A	0009152	biological_process	purine ribonucleotide biosynthetic process
A	0014850	biological_process	response to muscle activity
A	0016829	molecular_function	lyase activity
A	0032991	cellular_component	protein-containing complex
A	0042594	biological_process	response to starvation
A	0042802	molecular_function	identical protein binding
A	0044208	biological_process	'de novo' AMP biosynthetic process
A	0070626	molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
A	0097294	biological_process	'de novo' XMP biosynthetic process
B	0001666	biological_process	response to hypoxia
B	0003824	molecular_function	catalytic activity
B	0004018	molecular_function	N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006167	biological_process	AMP biosynthetic process
B	0006177	biological_process	GMP biosynthetic process
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0007584	biological_process	response to nutrient
B	0009060	biological_process	aerobic respiration
B	0009152	biological_process	purine ribonucleotide biosynthetic process
B	0014850	biological_process	response to muscle activity
B	0016829	molecular_function	lyase activity
B	0032991	cellular_component	protein-containing complex
B	0042594	biological_process	response to starvation
B	0042802	molecular_function	identical protein binding
B	0044208	biological_process	'de novo' AMP biosynthetic process
B	0070626	molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
B	0097294	biological_process	'de novo' XMP biosynthetic process
C	0001666	biological_process	response to hypoxia
C	0003824	molecular_function	catalytic activity
C	0004018	molecular_function	N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
C	0005829	cellular_component	cytosol
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0006167	biological_process	AMP biosynthetic process
C	0006177	biological_process	GMP biosynthetic process
C	0006189	biological_process	'de novo' IMP biosynthetic process
C	0007584	biological_process	response to nutrient
C	0009060	biological_process	aerobic respiration
C	0009152	biological_process	purine ribonucleotide biosynthetic process
C	0014850	biological_process	response to muscle activity
C	0016829	molecular_function	lyase activity
C	0032991	cellular_component	protein-containing complex
C	0042594	biological_process	response to starvation
C	0042802	molecular_function	identical protein binding
C	0044208	biological_process	'de novo' AMP biosynthetic process
C	0070626	molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
C	0097294	biological_process	'de novo' XMP biosynthetic process
D	0001666	biological_process	response to hypoxia
D	0003824	molecular_function	catalytic activity
D	0004018	molecular_function	N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
D	0005829	cellular_component	cytosol
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0006167	biological_process	AMP biosynthetic process
D	0006177	biological_process	GMP biosynthetic process
D	0006189	biological_process	'de novo' IMP biosynthetic process
D	0007584	biological_process	response to nutrient
D	0009060	biological_process	aerobic respiration
D	0009152	biological_process	purine ribonucleotide biosynthetic process
D	0014850	biological_process	response to muscle activity
D	0016829	molecular_function	lyase activity
D	0032991	cellular_component	protein-containing complex
D	0042594	biological_process	response to starvation
D	0042802	molecular_function	identical protein binding
D	0044208	biological_process	'de novo' AMP biosynthetic process
D	0070626	molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
D	0097294	biological_process	'de novo' XMP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE AMP A 1000

Chain	Residue
A	ARG85
A	ARG338
A	FUM1001
A	CL2001
A	HOH2054
A	HOH2251
A	HOH2252
A	HOH2253
B	HIS159
D	ARG20
D	TYR21
A	HIS86
D	MET299
D	ARG303
A	ASP87
A	SER112
A	GLN241
A	ARG329
A	LEU331
A	SER334
A	ALA335

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FUM A 1001

Chain	Residue
A	HIS86
A	MET89
A	THR111
A	SER112
A	GLN241
A	AMP1000
A	HOH2255
A	HOH2256
B	THR158
B	HIS159
D	LYS295

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1003

Chain	Residue
A	LYS35
A	TRP39
A	ASP87
A	GLY116
A	ASP120
A	SER334
A	ARG338
A	HOH2161
A	HOH2257

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 2001

Chain	Residue
A	AMP1000
D	ASN297
D	MET299

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 2002

Chain	Residue
A	THR111
A	TYR114
A	ARG196
A	LYS199
A	GLY200

site_id	AC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE 2SA B 1002

Chain	Residue
A	THR158
A	HIS159
B	ARG85
B	HIS86
B	ASP87
B	THR111
B	SER112
B	GLN241
B	ARG329
B	SER334
B	ALA335
B	ARG338
B	CL2001
B	HOH2038
B	HOH2051
B	HOH2130
B	HOH2161
B	HOH2163
B	HOH2165
B	HOH2166
C	ARG20
C	TYR21
C	LYS295
C	MET299
C	ARG303

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 1003

Chain	Residue
B	LYS35
B	ASP87
B	GLY116
B	ASP120
B	SER334
B	ARG338
B	HOH2168

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1004

Chain	Residue
B	ASP120
B	ARG337
B	ARG338
B	LEU341
B	ALA342
B	HOH2131

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 2001

Chain	Residue
B	2SA1002
B	HOH2166
C	ASN297

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL B 2002

Chain	Residue
B	THR111
B	TYR114
B	ARG196
B	LYS199
B	GLY200

site_id	BC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE AMP C 1000

Chain	Residue
C	ARG85
C	HIS86
C	ASP87
C	SER112
C	GLN241
C	ARG329
C	LEU331
C	SER334
C	ALA335
C	ARG338
C	FUM1001
C	HOH2241
C	HOH2242
C	HOH2243
D	HIS159
B	ARG20
B	TYR21
B	MET299
B	ARG303

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FUM C 1001

Chain	Residue
B	LYS295
B	ASN297
C	HIS86
C	THR111
C	SER112
C	GLN241
C	AMP1000
D	THR158
D	HIS159

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 1003

Chain	Residue
C	LYS35
C	TRP39
C	ASP87
C	GLY116
C	ASP120
C	SER334
C	ARG338
C	HOH2167
C	HOH2245

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 2002

Chain	Residue
C	TYR114
C	ARG196
C	LYS199
C	GLY200

site_id	BC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE 2SA D 1002

Chain	Residue
A	ARG20
A	TYR21
A	LYS295
A	MET299
A	ARG303
C	THR158
C	HIS159
D	ARG85
D	HIS86
D	ASP87
D	THR111
D	SER112
D	GLN241
D	ARG329
D	SER334
D	ALA335
D	ARG338
D	CL2001
D	HOH2067
D	HOH2087
D	HOH2244
D	HOH2245
D	HOH2246
D	HOH2247
D	HOH2249

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL D 1003

Chain	Residue
D	LYS35
D	TRP39
D	ASP87
D	GLY116
D	ASP120
D	SER334
D	ARG338
D	HOH2212
D	HOH2213
D	HOH2250

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL D 2001

Chain	Residue
A	ASN297
A	MET299
D	2SA1002
D	HOH2026

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D 2002

Chain	Residue
D	THR111
D	TYR114
D	ARG196
D	LYS199
D	GLY200

Functional Information from PROSITE/UniProt

site_id	PS00163
Number of Residues	10
Details	FUMARATE_LYASES Fumarate lyases signature. GSsaMpYKrN

Chain	Residue	Details
A	GLY288-ASN297

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"22812634","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"description":"in other chain"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
A	THR158
A	HIS159
C	GLU302
C	LYS295

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
D	GLU302
D	LYS295
B	THR158
B	HIS159

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
A	GLU302
A	LYS295
C	THR158
C	HIS159

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
D	THR158
D	HIS159
B	GLU302
B	LYS295

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