1J21

Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with ATP and citrulline

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	14
Details	BINDING SITE FOR RESIDUE ATP A 510

Chain	Residue
A	ALA6
A	ARG92
A	HIS113
A	GLY114
A	PHE125
A	HOH1453
A	SER8
A	GLY10
A	LEU11
A	ASP12
A	THR13
A	PHE31
A	ALA33
A	GLN37

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP B 1510

Chain	Residue
B	ALA6
B	SER8
B	GLY10
B	ASP12
B	THR13
B	PHE31
B	ALA33
B	GLN37
B	HIS113
B	GLY114
B	PHE125
B	HOH1334
B	HOH1417
B	HOH1435

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ATP C 2510

Chain	Residue
C	ALA6
C	SER8
C	GLY10
C	LEU11
C	ASP12
C	THR13
C	PHE31
C	THR32
C	ALA33
C	ARG92
C	HIS113
C	GLY114
C	PHE125

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP D 3510

Chain	Residue
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	HOH1355

---

site_id	AC5
Number of Residues	13
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	ASP175
A	SER182
A	GLU184
A	GLU258
A	TYR270
A	TYR310

---

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CIR B 1520

Chain	Residue
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

---

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CIR C 2520

Chain	Residue
C	TYR84
C	THR88
C	SER89
C	ASN120
C	ASP121
C	ARG124
C	SER173
C	MET174
C	ASP175
C	SER182
C	GLU184
C	GLU258
C	TYR270
C	TYR310

---

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CIR D 3520

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

---

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

---