Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5NX9

Crystal structure of Neanderthal Adenylosuccinate Lyase (ADSL) in complex with its products AMP and fumarate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0006189	biological_process	'de novo' IMP biosynthetic process
A	0009152	biological_process	purine ribonucleotide biosynthetic process
A	0016829	molecular_function	lyase activity
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
B	0000166	molecular_function	nucleotide binding
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	0006189	biological_process	'de novo' IMP biosynthetic process
B	0009152	biological_process	purine ribonucleotide biosynthetic process
B	0016829	molecular_function	lyase activity
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
C	0000166	molecular_function	nucleotide binding
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	0006189	biological_process	'de novo' IMP biosynthetic process
C	0009152	biological_process	purine ribonucleotide biosynthetic process
C	0016829	molecular_function	lyase activity
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
D	0000166	molecular_function	nucleotide binding
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	0006189	biological_process	'de novo' IMP biosynthetic process
D	0009152	biological_process	purine ribonucleotide biosynthetic process
D	0016829	molecular_function	lyase activity
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CL A 501

Chain	Residue
A	GLY200
A	THR201
A	SER207
A	HOH621

site_id	AC2
Number of Residues	4
Details	binding site for residue CL A 502

Chain	Residue
A	THR111
A	ARG196
A	LYS199
A	GLY200

site_id	AC3
Number of Residues	20
Details	binding site for residue AMP A 503

Chain	Residue
A	ARG85
A	HIS86
A	ASP87
A	SER112
A	GLN241
A	ARG329
A	LEU331
A	SER334
A	ALA335
A	ARG338
A	FUM504
A	HOH602
A	HOH623
B	HIS159
D	ARG20
D	TYR21
D	GLY288
D	MET299
D	ARG303
A	GLU81

site_id	AC4
Number of Residues	11
Details	binding site for residue FUM A 504

Chain	Residue
A	HIS86
A	THR111
A	SER112
A	GLN241
A	AMP503
B	THR158
B	HIS159
D	SER289
D	SER290
D	LYS295
D	ASN297

site_id	AC5
Number of Residues	3
Details	binding site for residue PEG A 505

Chain	Residue
A	GLN416
A	PEG507
C	VAL364

site_id	AC6
Number of Residues	5
Details	binding site for residue PEG A 506

Chain	Residue
A	GLU220
A	GLN221
A	LYS224
A	HOH638
C	ASP59

site_id	AC7
Number of Residues	8
Details	binding site for residue PEG A 507

Chain	Residue
A	ARG141
A	SER359
A	GLU360
A	LEU362
A	GLN416
A	PEG505
A	HOH605
A	HOH661

site_id	AC8
Number of Residues	2
Details	binding site for residue PEG A 508

Chain	Residue
A	GLN184
B	ARG234

site_id	AC9
Number of Residues	4
Details	binding site for residue PEG A 509

Chain	Residue
A	ARG372
A	GLN375
C	GLN375
C	VAL414

site_id	AD1
Number of Residues	4
Details	binding site for residue CL B 501

Chain	Residue
B	THR111
B	ARG196
B	LYS199
B	GLY200

site_id	AD2
Number of Residues	19
Details	binding site for residue 2SA B 502

Chain	Residue
A	THR158
A	HIS159
B	ARG85
B	HIS86
B	ASP87
B	THR111
B	SER112
B	GLN241
B	ARG329
B	LEU331
B	SER334
B	ALA335
B	ARG338
B	HOH638
C	ARG20
C	TYR21
C	ASN297
C	MET299
C	ARG303

site_id	AD3
Number of Residues	3
Details	binding site for residue PEG B 503

Chain	Residue
B	THR52
B	LYS229
B	HOH619

site_id	AD4
Number of Residues	25
Details	binding site for residue 2SA C 501

Chain	Residue
C	THR111
C	SER112
C	GLN241
C	ARG329
C	SER334
C	ALA335
C	ARG338
C	HOH616
C	HOH623
C	HOH625
C	HOH631
D	THR158
D	HIS159
B	ARG20
B	TYR21
B	GLY288
B	SER289
B	SER290
B	LYS295
B	ASN297
B	MET299
B	ARG303
C	ARG85
C	HIS86
C	ASP87

site_id	AD5
Number of Residues	2
Details	binding site for residue CL C 502

Chain	Residue
C	THR201
C	SER207

site_id	AD6
Number of Residues	4
Details	binding site for residue CL C 503

Chain	Residue
C	THR111
C	ARG196
C	LYS199
C	GLY200

site_id	AD7
Number of Residues	5
Details	binding site for residue PEG C 504

Chain	Residue
A	ASP59
C	HIS217
C	GLU220
C	GLN221
C	LYS224

site_id	AD8
Number of Residues	3
Details	binding site for residue PEG C 505

Chain	Residue
A	THR58
C	ASP215
C	HIS217

site_id	AD9
Number of Residues	5
Details	binding site for residue PEG C 506

Chain	Residue
B	TYR34
B	THR38
B	GLU70
C	GLU60
C	LYS101

site_id	AE1
Number of Residues	4
Details	binding site for residue GOL C 507

Chain	Residue
C	LEU53
C	GLY54
C	PHE212
C	GLU213

site_id	AE2
Number of Residues	3
Details	binding site for residue PEG C 508

Chain	Residue
C	GLN210
D	ASN384
D	SER448

site_id	AE3
Number of Residues	5
Details	binding site for residue CL D 501

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

site_id	AE4
Number of Residues	17
Details	binding site for residue AMP D 502

Chain	Residue
A	ARG20
A	TYR21
A	ARG303
C	HIS159
D	ARG85
D	HIS86
D	ASP87
D	SER112
D	GLN241
D	ARG329
D	LEU331
D	SER334
D	ALA335
D	ARG338
D	FUM503
D	HOH612
D	HOH627

site_id	AE5
Number of Residues	10
Details	binding site for residue FUM D 503

Chain	Residue
A	GLY288
A	LYS295
A	ASN297
C	THR158
C	HIS159
D	HIS86
D	THR111
D	SER112
D	GLN241
D	AMP502

site_id	AE6
Number of Residues	1
Details	binding site for residue PEG D 504

Chain	Residue
D	LYS402

site_id	AE7
Number of Residues	3
Details	binding site for residue PEG D 505

Chain	Residue
A	ARG14
D	PHE74
D	ALA78

site_id	AE8
Number of Residues	2
Details	binding site for residue PEG D 506

Chain	Residue
D	ARG85
D	HOH667

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

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