2NZ2

Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000050	biological_process	urea cycle
A	0001822	biological_process	kidney development
A	0001889	biological_process	liver development
A	0003723	molecular_function	RNA binding
A	0004055	molecular_function	argininosuccinate synthase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005741	cellular_component	mitochondrial outer membrane
A	0005829	cellular_component	cytosol
A	0006526	biological_process	L-arginine biosynthetic process
A	0006533	biological_process	L-aspartate catabolic process
A	0006953	biological_process	acute-phase response
A	0007494	biological_process	midgut development
A	0007584	biological_process	response to nutrient
A	0007623	biological_process	circadian rhythm
A	0009410	biological_process	response to xenobiotic stimulus
A	0009636	biological_process	response to toxic substance
A	0010043	biological_process	response to zinc ion
A	0010046	biological_process	response to mycotoxin
A	0014075	biological_process	response to amine
A	0015643	molecular_function	toxic substance binding
A	0016597	molecular_function	amino acid binding
A	0019241	biological_process	L-citrulline catabolic process
A	0032355	biological_process	response to estradiol
A	0032496	biological_process	response to lipopolysaccharide
A	0042802	molecular_function	identical protein binding
A	0043025	cellular_component	neuronal cell body
A	0043200	biological_process	response to amino acid
A	0043204	cellular_component	perikaryon
A	0043434	biological_process	response to peptide hormone
A	0045429	biological_process	positive regulation of nitric oxide biosynthetic process
A	0048545	biological_process	response to steroid hormone
A	0051384	biological_process	response to glucocorticoid
A	0060416	biological_process	response to growth hormone
A	0060539	biological_process	diaphragm development
A	0070062	cellular_component	extracellular exosome
A	0070542	biological_process	response to fatty acid
A	0070852	cellular_component	cell body fiber
A	0071222	biological_process	cellular response to lipopolysaccharide
A	0071230	biological_process	cellular response to amino acid stimulus
A	0071242	biological_process	cellular response to ammonium ion
A	0071320	biological_process	cellular response to cAMP
A	0071346	biological_process	cellular response to type II interferon
A	0071356	biological_process	cellular response to tumor necrosis factor
A	0071377	biological_process	cellular response to glucagon stimulus
A	0071400	biological_process	cellular response to oleic acid
A	0071418	biological_process	cellular response to amine stimulus
A	0071499	biological_process	cellular response to laminar fluid shear stress
A	0071549	biological_process	cellular response to dexamethasone stimulus
A	1903038	biological_process	negative regulation of leukocyte cell-cell adhesion

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE NA A 503

Chain	Residue
A	GLN107

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASP A 501

Chain	Residue
A	HOH569
A	HOH664
A	ALA118
A	THR119
A	GLY122
A	ASN123
A	ASP124
A	GLU191
A	CIR502
A	HOH511

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIR A 502

Chain	Residue
A	TYR87
A	THR91
A	ASN123
A	ASP124
A	ARG127
A	SER180
A	MET181
A	ASP182
A	SER189
A	GLU191
A	GLU270
A	TYR282
A	ASP501
A	HOH569
A	HOH647

---

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	ALA10-SER18

---

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

Chain	Residue	Details
A	GLY117-PHE128

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	17
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18323623","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09034","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16460","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; by CLOCK","evidences":[{"source":"PubMed","id":"28985504","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

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	ARG95
A	ASP124

---