Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1J1Z

Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with substrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000050	biological_process	urea cycle
A	0000053	biological_process	argininosuccinate metabolic process
A	0000166	molecular_function	nucleotide binding
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	0008652	biological_process	amino acid biosynthetic process
A	0016874	molecular_function	ligase activity
B	0000050	biological_process	urea cycle
B	0000053	biological_process	argininosuccinate metabolic process
B	0000166	molecular_function	nucleotide binding
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	0008652	biological_process	amino acid biosynthetic process
B	0016874	molecular_function	ligase activity
C	0000050	biological_process	urea cycle
C	0000053	biological_process	argininosuccinate metabolic process
C	0000166	molecular_function	nucleotide binding
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	0008652	biological_process	amino acid biosynthetic process
C	0016874	molecular_function	ligase activity
D	0000050	biological_process	urea cycle
D	0000053	biological_process	argininosuccinate metabolic process
D	0000166	molecular_function	nucleotide binding
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	0008652	biological_process	amino acid biosynthetic process
D	0016874	molecular_function	ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP A 510

Chain	Residue
A	ALA6
A	HIS113
A	GLY114
A	PHE125
A	SER173
A	ASP175
A	CIR520
A	ASP530
A	SER8
A	ASP12
A	THR13
A	PHE31
A	THR32
A	ALA33
A	GLN37
A	ARG92

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP B 2510

Chain	Residue
A	ASP2530
B	ALA6
B	TYR7
B	SER8
B	GLY10
B	ASP12
B	THR13
B	PHE31
B	THR32
B	ALA33
B	GLN37
B	ARG92
B	HIS113
B	GLY114
B	PHE125
B	HOH1506

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP C 3510

Chain	Residue
A	ASP3530
C	ALA6
C	SER8
C	ASP12
C	THR13
C	PHE31
C	THR32
C	ALA33
C	GLN37
C	ARG92
C	ILE95
C	HIS113
C	GLY114
C	ALA115
C	PHE125
C	SER173
C	ASP175
C	HOH1541
C	CIR3520

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP D 4510

Chain	Residue
A	ASP4530
D	ALA6
D	TYR7
D	SER8
D	GLY10
D	LEU11
D	ASP12
D	THR13
D	PHE31
D	ALA33
D	GLN37
D	ARG92
D	HIS113
D	GLY114
D	PHE125
D	HOH1479
D	CIR4520

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIR A 520

Chain	Residue
A	TYR84
A	THR88
A	SER89
A	ASN120
A	ARG124
A	SER173
A	MET174
A	SER182
A	GLU184
A	GLU258
A	TYR270
A	TYR310
A	ATP510
A	ASP530
A	HOH1017

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIR B 2520

Chain	Residue
A	ASP2530
B	TYR84
B	THR88
B	SER89
B	ASN120
B	ARG124
B	SER173
B	MET174
B	ASP175
B	SER182
B	GLU184
B	GLU258
B	TYR270
B	TYR310
B	HOH1039

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIR C 3520

Chain	Residue
C	TYR84
C	THR88
C	SER89
C	ASN120
C	ASP121
C	ARG124
C	SER173
C	MET174
C	SER182
C	GLU184
C	GLU258
C	TYR270
C	TYR310
C	ATP3510
A	ASP3530

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CIR D 4520

Chain	Residue
A	HOH1124
A	ASP4530
D	TYR84
D	THR88
D	SER89
D	ASN120
D	ARG124
D	SER173
D	MET174
D	ASP175
D	SER182
D	GLU184
D	GLU258
D	TYR270
D	TYR310
D	ATP4510

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASP A 530

Chain	Residue
A	ALA115
A	THR116
A	GLY119
A	ASN120
A	ASP121
A	ATP510
A	CIR520
A	HOH1017
A	HOH1071
A	HOH1159

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASP A 2530

Chain	Residue
A	HOH1049
B	ALA115
B	THR116
B	GLY119
B	ASN120
B	ASP121
B	HOH1039
B	HOH1099
B	ATP2510
B	CIR2520

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASP A 3530

Chain	Residue
A	HOH1004
A	HOH1117
C	ALA115
C	THR116
C	GLY119
C	ASN120
C	ASP121
C	HOH1028
C	ATP3510
C	CIR3520

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ASP A 4530

Chain	Residue
A	HOH1124
A	HOH1161
D	ALA115
D	THR116
D	GLY119
D	ASN120
D	ASP121
D	GLU184
D	HOH1212
D	ATP4510
D	CIR4520

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	ALA6-SER14

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

Chain	Residue	Details
A	GLY114-PHE125

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00005, ECO:0000269\|PubMed:11844799, ECO:0000269\|PubMed:12684518

Chain	Residue	Details
A	ALA6
D	ALA6
D	ALA33
D	GLY114
A	ALA33
A	GLY114
B	ALA6
B	ALA33
B	GLY114
C	ALA6
C	ALA33
C	GLY114

site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING:

Chain	Residue	Details
A	TYR84
A	TYR270
B	TYR84
B	SER89
B	THR116
B	ASN120
B	ASP121
B	ARG124
B	SER173
B	SER182
B	GLU258
A	SER89
B	TYR270
C	TYR84
C	SER89
C	THR116
C	ASN120
C	ASP121
C	ARG124
C	SER173
C	SER182
C	GLU258
A	THR116
C	TYR270
D	TYR84
D	SER89
D	THR116
D	ASN120
D	ASP121
D	ARG124
D	SER173
D	SER182
D	GLU258
A	ASN120
D	TYR270
A	ASP121
A	ARG124
A	SER173
A	SER182
A	GLU258

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 316

Chain	Residue	Details
A	ASP12	steric role
A	ARG92	electrostatic stabiliser, hydrogen bond donor
A	ASP121	proton acceptor, proton donor
A	SER173	hydrogen bond donor, steric role

site_id	MCSA2
Number of Residues	4
Details	M-CSA 316

Chain	Residue	Details
B	ASP12	steric role
B	ARG92	electrostatic stabiliser, hydrogen bond donor
B	ASP121	proton acceptor, proton donor
B	SER173	hydrogen bond donor, steric role

site_id	MCSA3
Number of Residues	4
Details	M-CSA 316

Chain	Residue	Details
C	ASP12	steric role
C	ARG92	electrostatic stabiliser, hydrogen bond donor
C	ASP121	proton acceptor, proton donor
C	SER173	hydrogen bond donor, steric role

site_id	MCSA4
Number of Residues	4
Details	M-CSA 316

Chain	Residue	Details
D	ASP12	steric role
D	ARG92	electrostatic stabiliser, hydrogen bond donor
D	ASP121	proton acceptor, proton donor
D	SER173	hydrogen bond donor, steric role

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