Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XNQ

Crystal Structure of Argininosuccinate synthase from Legionella pneumophila Philadelphia 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000050	biological_process	urea cycle
A	0000053	biological_process	argininosuccinate metabolic process
A	0004055	molecular_function	argininosuccinate synthase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	arginine biosynthetic process
A	0016874	molecular_function	ligase activity
B	0000050	biological_process	urea cycle
B	0000053	biological_process	argininosuccinate metabolic process
B	0004055	molecular_function	argininosuccinate synthase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006526	biological_process	arginine biosynthetic process
B	0016874	molecular_function	ligase activity
C	0000050	biological_process	urea cycle
C	0000053	biological_process	argininosuccinate metabolic process
C	0004055	molecular_function	argininosuccinate synthase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006526	biological_process	arginine biosynthetic process
C	0016874	molecular_function	ligase activity
D	0000050	biological_process	urea cycle
D	0000053	biological_process	argininosuccinate metabolic process
D	0004055	molecular_function	argininosuccinate synthase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006526	biological_process	arginine biosynthetic process
D	0016874	molecular_function	ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue EDO A 501

Chain	Residue
A	GLU217
A	GLU218
A	HOH605

site_id	AC2
Number of Residues	7
Details	binding site for residue EDO A 502

Chain	Residue
B	EDO504
A	TYR63
A	VAL64
A	HOH781
A	HOH795
B	TYR63
B	VAL65

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

Chain	Residue
A	SER13
A	GLY15
A	ASP17
A	THR18
A	GLY119
A	HOH830

site_id	AC4
Number of Residues	11
Details	binding site for residue SO4 A 504

Chain	Residue
A	THR296
A	SER298
A	HOH604
A	HOH628
A	HOH757
A	HOH778
C	SER391
C	ALA392
C	HOH747
D	TYR132
D	HOH742

site_id	AC5
Number of Residues	11
Details	binding site for residue SO4 B 501

Chain	Residue
A	SER391
A	ALA392
A	HOH724
B	TYR132
B	HOH602
B	HOH613
B	HOH653
B	HOH724
B	HOH745
C	THR296
C	SER298

site_id	AC6
Number of Residues	5
Details	binding site for residue SO4 B 502

Chain	Residue
B	GLY15
B	LEU16
B	ARG155
B	HOH695
B	HOH783

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO B 503

Chain	Residue
B	GLU217
B	GLU218

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO B 504

Chain	Residue
A	ALA62
A	EDO502
A	HOH765
B	LYS103
B	GLU106
B	HOH647
B	HOH792

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO B 505

Chain	Residue
A	LYS61
A	GLU111
B	GLN102
B	HOH668

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO B 506

Chain	Residue
B	SER13
B	GLY15
B	ASP17
B	THR18
B	GLY119

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO B 507

Chain	Residue
B	TRP24
B	HIS28
B	TRP150
B	ASP151

site_id	AD3
Number of Residues	11
Details	binding site for residue SO4 C 501

Chain	Residue
B	THR296
B	SER298
C	TYR132
C	HOH603
C	HOH646
C	HOH677
C	HOH706
C	HOH774
D	SER391
D	ALA392
D	HOH744

site_id	AD4
Number of Residues	5
Details	binding site for residue SO4 C 502

Chain	Residue
C	GLY15
C	LEU16
C	ARG155
C	PRO170
C	HOH736

site_id	AD5
Number of Residues	2
Details	binding site for residue EDO C 503

Chain	Residue
C	GLU217
C	GLU218

site_id	AD6
Number of Residues	7
Details	binding site for residue EDO C 504

Chain	Residue
C	TYR63
C	VAL64
C	HOH687
C	HOH803
D	TYR63
D	VAL65
D	EDO504

site_id	AD7
Number of Residues	6
Details	binding site for residue EDO C 505

Chain	Residue
C	SER13
C	GLY15
C	ASP17
C	THR18
C	GLY119
C	HOH690

site_id	AD8
Number of Residues	4
Details	binding site for residue EDO C 506

Chain	Residue
C	ASP151
C	TRP24
C	HIS28
C	TRP150

site_id	AD9
Number of Residues	10
Details	binding site for residue SO4 D 501

Chain	Residue
A	TYR132
B	SER391
B	ALA392
D	THR296
D	SER298
D	HOH602
D	HOH700
D	HOH718
D	HOH721
D	HOH738

site_id	AE1
Number of Residues	4
Details	binding site for residue SO4 D 502

Chain	Residue
D	GLY15
D	LEU16
D	ARG155
D	HOH614

site_id	AE2
Number of Residues	5
Details	binding site for residue EDO D 503

Chain	Residue
C	SER212
D	ASP216
D	GLU217
D	GLU218
D	HOH642

site_id	AE3
Number of Residues	7
Details	binding site for residue EDO D 504

Chain	Residue
C	LYS61
C	ALA62
C	EDO504
C	HOH759
D	LYS103
D	GLU106
D	HOH680

site_id	AE4
Number of Residues	5
Details	binding site for residue EDO D 505

Chain	Residue
D	SER13
D	GLY15
D	ASP17
D	THR18
D	GLY119

Functional Information from PROSITE/UniProt

site_id	PS00564
Number of Residues	9
Details	ARGININOSUCCIN_SYN_1 Argininosuccinate synthase signature 1. AYSGGLDTS

Chain	Residue	Details
A	ALA11-SER19

site_id	PS00565
Number of Residues	12
Details	ARGININOSUCCIN_SYN_2 Argininosuccinate synthase signature 2. GaTgKGNDqvRF

Chain	Residue	Details
A	GLY119-PHE130

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00005

Chain	Residue	Details
A	ASN125
A	ASP126
A	ARG129
A	SER178
A	SER187
A	GLU263
A	TYR275
B	ALA11
B	TYR90
B	GLY119
B	THR121
B	ASN125
B	ASP126
B	ARG129
B	SER178
B	SER187
B	GLU263
B	TYR275
C	ALA11
C	TYR90
C	GLY119
C	THR121
C	ASN125
C	ASP126
C	ARG129
C	SER178
C	SER187
C	GLU263
C	TYR275
D	ALA11
D	TYR90
D	GLY119
D	THR121
D	ASN125
D	ASP126
D	ARG129
D	SER178
D	SER187
D	GLU263
D	TYR275
A	ALA11
A	TYR90
A	GLY119
A	THR121

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