4EFC

Crystal Structure of Adenylosuccinate Lyase from Trypanosoma Brucei, Tb427tmp.160.5560

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	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0006163	biological_process	purine nucleotide metabolic process
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006188	biological_process	IMP 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	0020015	cellular_component	glycosome
A	0044208	biological_process	'de novo' AMP biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0070626	molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
A	0097740	cellular_component	paraflagellar rod
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	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0006163	biological_process	purine nucleotide metabolic process
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006188	biological_process	IMP 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	0020015	cellular_component	glycosome
B	0044208	biological_process	'de novo' AMP biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0070626	molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
B	0097740	cellular_component	paraflagellar rod

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE AMP A 501

Chain	Residue
A	ASN106
A	THR356
A	ARG359
A	HOH605
A	HOH606
A	HOH627
A	HOH673
A	HOH700
A	HOH870
B	ARG29
B	TYR30
A	HIS107
B	GLY309
B	ILE320
B	ASN324
B	EDO502
A	ASP108
A	SER138
A	GLN139
A	HIS185
A	GLN262
A	ARG350
A	SER355

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	ASP285
A	ASP289
A	SER346
A	LEU348
A	HOH691

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	SER310
A	MET313
A	LYS316
A	ASN318
B	THR184
B	HIS185
B	GLN262
B	AMP501

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 504

Chain	Residue
A	ARG72
A	HOH954
A	HOH972
A	HOH973

---

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE AMP B 501

Chain	Residue
A	ARG29
A	TYR30
A	GLY309
A	ILE320
A	ASN324
A	EDO503
B	ASN106
B	HIS107
B	ASP108
B	SER138
B	GLN139
B	HIS185
B	GLN262
B	ARG350
B	LEU352
B	SER355
B	THR356
B	ARG359
B	HOH613
B	HOH627
B	HOH644
B	HOH655
B	HOH672
B	HOH736

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 502

Chain	Residue
A	THR184
A	HIS185
A	GLN262
A	AMP501
B	SER310
B	MET313
B	LYS316
B	ASN318

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 503

Chain	Residue
B	ASP285
B	ASP289
B	SER346
B	LEU348
B	HOH897

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 504

Chain	Residue
B	ASP274
B	ASN337
B	HOH639
B	HOH661
B	HOH664
B	HOH664

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY309-ASN318

---

site_id	PS00308
Number of Residues	10
Details	LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. VTEFVHFGLT

Chain	Residue	Details
A	VAL128-THR137

---