Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1J20

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

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	L-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	L-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	L-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	L-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	5
Details	BINDING SITE FOR RESIDUE SO4 A 540

Chain	Residue
A	SER8
A	GLY10
A	THR13
A	AMP510
A	HOH1854

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 2540

Chain	Residue
B	AMP2510
B	SER8
B	GLY10
B	THR13
B	HOH1705

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 3540

Chain	Residue
C	SER8
C	GLY10
C	THR13
C	HOH1846
C	AMP3510

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 4540

Chain	Residue
D	SER8
D	GLY10
D	ASP12
D	THR13
D	HOH1579
D	HOH1740
D	AMP4510

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AMP A 510

Chain	Residue
A	ALA6
A	THR13
A	PHE31
A	ALA33
A	GLN37
A	ARG92
A	HIS113
A	GLY114
A	PHE125
A	MET174
A	ASP175
A	AS1520
A	SO4540

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AMP B 2510

Chain	Residue
B	ALA6
B	TYR7
B	THR13
B	PHE31
B	ALA33
B	GLN37
B	ARG92
B	HIS113
B	GLY114
B	PHE125
B	AS12520
B	SO42540

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AMP C 3510

Chain	Residue
C	ALA6
C	THR13
C	PHE31
C	ALA33
C	GLN37
C	ARG92
C	ILE95
C	HIS113
C	GLY114
C	PHE125
C	ASP175
C	SO43540

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AMP D 4510

Chain	Residue
D	ALA6
D	TYR7
D	THR13
D	PHE31
D	ALA33
D	GLN37
D	ARG92
D	GLY114
D	PHE125
D	ASP175
D	AS14520
D	SO44540

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE AS1 A 520

Chain	Residue
A	TYR84
A	THR88
A	SER89
A	ALA115
A	THR116
A	GLY119
A	ASN120
A	ASP121
A	ARG124
A	SER182
A	GLU184
A	GLU258
A	ARG260
A	TYR270
A	TYR310
A	AMP510
A	HOH1013
A	HOH1017
A	HOH1221

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AS1 B 2520

Chain	Residue
B	SER182
B	GLU184
B	GLU258
B	TYR270
B	TYR310
B	HOH1050
B	AMP2510
B	TYR84
B	THR88
B	SER89
B	ALA115
B	THR116
B	GLY119
B	ASN120
B	ASP121
B	ARG124

site_id	BC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE AS1 C 3520

Chain	Residue
C	TYR84
C	THR88
C	SER89
C	ALA115
C	THR116
C	GLY119
C	ASN120
C	ASP121
C	ARG124
C	SER182
C	GLU184
C	GLU258
C	ARG260
C	TYR270
C	TYR310
C	HOH1022
C	HOH1036
C	HOH1092

site_id	BC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE AS1 D 4520

Chain	Residue
D	TYR84
D	THR88
D	SER89
D	ALA115
D	THR116
D	GLY119
D	ASN120
D	ASP121
D	ARG124
D	SER182
D	GLU184
D	GLU258
D	ARG260
D	TYR270
D	TYR310
D	HOH1059
D	HOH1094
D	AMP4510

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	40
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00005","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11844799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12684518","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1kp2

Chain	Residue	Details
A	ASP121
A	ARG92

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1kp2

Chain	Residue	Details
B	ASP121
B	ARG92

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1kp2

Chain	Residue	Details
C	ASP121
C	ARG92

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1kp2

Chain	Residue	Details
D	ASP121
D	ARG92

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)