Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2J91

Crystal structure of Human Adenylosuccinate Lyase in complex with AMP

Replaces: 2J84

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	0009168	biological_process	purine ribonucleoside monophosphate 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	0044209	biological_process	AMP salvage
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	0009168	biological_process	purine ribonucleoside monophosphate 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	0044209	biological_process	AMP salvage
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	0009168	biological_process	purine ribonucleoside monophosphate 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	0044209	biological_process	AMP salvage
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	0009168	biological_process	purine ribonucleoside monophosphate 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	0044209	biological_process	AMP salvage
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	5
Details	BINDING SITE FOR RESIDUE CL A1001

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

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B1001

Chain	Residue
B	THR111
B	ARG196
B	LYS199
B	GLY200

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C1001

Chain	Residue
C	THR111
C	TYR114
C	ARG196
C	LYS199
C	GLY200

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D1001

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

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE AMP A1000

Chain	Residue
A	ARG20
A	TYR21
A	MET299
A	ARG303
A	HOH2245
A	HOH2331
A	HOH2332
C	HIS159
D	ARG85
D	HIS86
D	ASP87
D	GLN241
D	ARG329
D	LEU331
D	SER334
D	ALA335
D	ARG338
D	HOH2073
D	HOH2270

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE AMP B1000

Chain	Residue
B	ARG20
B	TYR21
B	MET299
B	ARG303
B	HOH2240
B	HOH2371
B	HOH2372
B	HOH2374
B	HOH2375
C	ARG85
C	HIS86
C	ASP87
C	SER112
C	GLN241
C	ARG329
C	LEU331
C	SER334
C	ALA335
C	ARG338
C	HOH2119
C	HOH2122
C	HOH2147
D	HIS159

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AMP C1000

Chain	Residue
A	HIS159
B	ARG85
B	ASP87
B	GLN241
B	ARG329
B	SER334
B	ALA335
B	ARG338
C	ARG20
C	TYR21
C	MET299
C	ARG303
C	HOH2370
C	HOH2371

site_id	AC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE AMP D1000

Chain	Residue
A	ARG85
A	HIS86
A	ASP87
A	SER112
A	GLN241
A	ARG329
A	LEU331
A	SER334
A	ALA335
A	ARG338
A	HOH2106
A	HOH2262
B	HIS159
B	GLU481
D	ARG20
D	TYR21
D	MET299
D	ARG303
D	HOH2406
D	HOH2407
D	HOH2409
D	HOH2410

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A1475

Chain	Residue
A	ASP87
A	GLY116
A	ASP120
A	SER334
A	ARG338
A	HOH2261
A	HOH2333
A	HOH2334
A	LYS35
A	TRP39

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B1482

Chain	Residue
B	PHE30
B	ASP120
B	ARG337
B	ARG338
B	LEU341
B	ALA342
B	HOH2259
B	HOH2376
B	HOH2377

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C1473

Chain	Residue
C	LYS35
C	TRP39
C	ASP87
C	GLY116
C	ASP120
C	SER334
C	ARG338
C	HOH2306
C	HOH2372
C	HOH2373

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D1474

Chain	Residue
B	GLN161
B	LYS415
D	LYS276
D	TYR294
D	LYS295
D	ARG296
D	HOH2411

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	8
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269\|PubMed:22812634

Chain	Residue	Details
A	HIS159
A	SER289
B	HIS159
B	SER289
C	HIS159
C	SER289
D	HIS159
D	SER289

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	ARG20
A	ARG303
B	ARG20
B	ARG303
C	ARG20
C	ARG303
D	ARG20
D	ARG303

site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: in other chain

Chain	Residue	Details
A	ARG85
B	ARG329
B	SER334
B	ARG338
C	ARG85
C	THR111
C	GLN241
C	ARG329
C	SER334
C	ARG338
D	ARG85
A	THR111
D	THR111
D	GLN241
D	ARG329
D	SER334
D	ARG338
A	GLN241
A	ARG329
A	SER334
A	ARG338
B	ARG85
B	THR111
B	GLN241

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N-acetylalanine => ECO:0000269\|Ref.8

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS147
A	LYS295
B	LYS147
B	LYS295
C	LYS147
C	LYS295
D	LYS147
D	LYS295

site_id	SWS_FT_FI6
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744\|PubMed:25114211

Chain	Residue	Details
A	LYS415
B	LYS415
C	LYS415
D	LYS415

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