Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5HW2

Crystal Structure of Adenylosuccinate Lyase from Francisella tularensis Complexed with fumaric acid

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	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	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	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	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	6
Details	binding site for residue K A 501

Chain	Residue
A	ASP96
A	GLN179
A	SER181
A	GLY182
A	THR211
A	GLN212

site_id	AC2
Number of Residues	6
Details	binding site for residue FUM A 502

Chain	Residue
A	THR93
A	SER94
A	HOH646
A	HIS67
A	HIS89
A	VAL92

site_id	AC3
Number of Residues	6
Details	binding site for residue PO4 A 503

Chain	Residue
A	ARG4
A	TYR5
A	ASN276
A	HOH695
D	SER306
D	ARG310

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 504

Chain	Residue
A	GLU309
A	HOH624
A	HOH716

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO A 505

Chain	Residue
A	GLU9
A	LYS12
A	ILE13
A	ASN18
A	HOH632

site_id	AC6
Number of Residues	6
Details	binding site for residue K B 501

Chain	Residue
B	THR93
B	ASP96
B	GLN179
B	GLY182
B	THR211
B	GLN212

site_id	AC7
Number of Residues	7
Details	binding site for residue FUM B 502

Chain	Residue
B	HIS67
B	THR93
B	SER94
B	GLN212
B	HOH629
B	HOH735
C	SER262

site_id	AC8
Number of Residues	8
Details	binding site for residue PO4 B 503

Chain	Residue
B	ARG4
B	TYR5
B	ASN276
B	HOH615
B	HOH628
B	HOH637
C	SER306
C	ARG310

site_id	AC9
Number of Residues	7
Details	binding site for residue K C 501

Chain	Residue
C	THR93
C	ASP96
C	GLN179
C	SER181
C	GLY182
C	THR211
C	GLN212

site_id	AD1
Number of Residues	2
Details	binding site for residue FUM C 502

Chain	Residue
C	THR93
C	SER94

site_id	AD2
Number of Residues	8
Details	binding site for residue PO4 C 503

Chain	Residue
B	SER306
B	ARG310
C	ARG4
C	TYR5
C	ASN276
C	HOH651
C	HOH653
C	HOH654

site_id	AD3
Number of Residues	4
Details	binding site for residue EDO C 504

Chain	Residue
C	LYS19
C	SER306
C	GLU309
C	HOH634

site_id	AD4
Number of Residues	5
Details	binding site for residue EDO C 505

Chain	Residue
C	GLN337
C	ARG338
C	ASP339
C	ILE340
C	HOH685

site_id	AD5
Number of Residues	6
Details	binding site for residue K D 501

Chain	Residue
D	ASP96
D	GLN179
D	SER181
D	GLY182
D	THR211
D	GLN212

site_id	AD6
Number of Residues	8
Details	binding site for residue PO4 D 502

Chain	Residue
A	SER306
A	ARG310
D	ARG4
D	TYR5
D	ASN276
D	HOH605
D	HOH623
D	HOH638

site_id	AD7
Number of Residues	3
Details	binding site for residue EDO D 503

Chain	Residue
D	LYS19
D	SER306
D	GLU309

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY261-ASN270

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