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2NZ2

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0000052biological_processcitrulline metabolic process
A0000053biological_processargininosuccinate metabolic process
A0000166molecular_functionnucleotide binding
A0001822biological_processkidney development
A0001889biological_processliver development
A0003723molecular_functionRNA binding
A0004055molecular_functionargininosuccinate synthase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005829cellular_componentcytosol
A0006526biological_processL-arginine biosynthetic process
A0006531biological_processaspartate metabolic process
A0006953biological_processacute-phase response
A0007494biological_processmidgut development
A0007584biological_processresponse to nutrient
A0007623biological_processcircadian rhythm
A0008652biological_processamino acid biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0010043biological_processresponse to zinc ion
A0010046biological_processresponse to mycotoxin
A0014075biological_processresponse to amine
A0015643molecular_functiontoxic substance binding
A0016597molecular_functionamino acid binding
A0016874molecular_functionligase activity
A0032355biological_processresponse to estradiol
A0032496biological_processresponse to lipopolysaccharide
A0042802molecular_functionidentical protein binding
A0043025cellular_componentneuronal cell body
A0043200biological_processresponse to amino acid
A0043204cellular_componentperikaryon
A0043434biological_processresponse to peptide hormone
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0048545biological_processresponse to steroid hormone
A0051384biological_processresponse to glucocorticoid
A0060416biological_processresponse to growth hormone
A0060539biological_processdiaphragm development
A0070062cellular_componentextracellular exosome
A0070542biological_processresponse to fatty acid
A0070852cellular_componentcell body fiber
A0071222biological_processcellular response to lipopolysaccharide
A0071230biological_processcellular response to amino acid stimulus
A0071242biological_processcellular response to ammonium ion
A0071320biological_processcellular response to cAMP
A0071346biological_processcellular response to type II interferon
A0071356biological_processcellular response to tumor necrosis factor
A0071377biological_processcellular response to glucagon stimulus
A0071400biological_processcellular response to oleic acid
A0071418biological_processcellular response to amine stimulus
A0071499biological_processcellular response to laminar fluid shear stress
A0071549biological_processcellular response to dexamethasone stimulus
A1903038biological_processnegative regulation of leukocyte cell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 503
ChainResidue
AGLN107

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ASP A 501
ChainResidue
AHOH569
AHOH664
AALA118
ATHR119
AGLY122
AASN123
AASP124
AGLU191
ACIR502
AHOH511

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CIR A 502
ChainResidue
ATYR87
ATHR91
AASN123
AASP124
AARG127
ASER180
AMET181
AASP182
ASER189
AGLU191
AGLU270
ATYR282
AASP501
AHOH569
AHOH647

Functional Information from PROSITE/UniProt
site_idPS00564
Number of Residues9
DetailsARGININOSUCCIN_SYN_1 Argininosuccinate synthase signature 1. AYSGGLDTS
ChainResidueDetails
AALA10-SER18

site_idPS00565
Number of Residues12
DetailsARGININOSUCCIN_SYN_2 Argininosuccinate synthase signature 2. GaTgKGNDqvRF
ChainResidueDetails
AGLY117-PHE128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18323623","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09034","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16460","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; by CLOCK","evidences":[{"source":"PubMed","id":"28985504","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
AARG95
AASP124

246031

PDB entries from 2025-12-10

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