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1KP2

Crystal Structure of E. coli Argininosuccinate Synthetase in Complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0000053biological_processargininosuccinate metabolic process
A0000166molecular_functionnucleotide binding
A0004055molecular_functionargininosuccinate synthase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006526biological_processL-arginine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0016874molecular_functionligase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 456
ChainResidue
ATYR98
AHOH499
ATHR102
APRO103
AASN134
AARG138
AGLU202
AGLU279
ATYR291
ATYR331

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 457
ChainResidue
ASER18
AGLY20
AASP22
ATHR23
AATP459

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 458
ChainResidue
AGLU262
AARG269
AHOH726

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP A 459
ChainResidue
AALA16
ATYR40
AALA42
AASP127
AGLY128
ASER129
ATHR130
AASP135
APHE139
AASP193
APO4457
AHOH559
AHOH632
AHOH642
AHOH741

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GAI A 460
ChainResidue
AMET60
AALA64
AGLU65
AASN210
ASER211
AHOH745

Functional Information from PROSITE/UniProt
site_idPS00564
Number of Residues9
DetailsARGININOSUCCIN_SYN_1 Argininosuccinate synthase signature 1. AFSGGLDTS
ChainResidueDetails
AALA16-SER24

site_idPS00565
Number of Residues12
DetailsARGININOSUCCIN_SYN_2 Argininosuccinate synthase signature 2. GsTyKGNDieRF
ChainResidueDetails
AGLY128-PHE139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11809762
ChainResidueDetails
APHE17
AASN43
ASER129
ASER194

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:11738042, ECO:0000269|PubMed:11809762
ChainResidueDetails
APHE99
AASP135
APHE139
ATHR192
AHIS201
AALA203
AASN280

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11738042
ChainResidueDetails
ATYR131
AILE136

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 11809762
ChainResidueDetails
AASP135
AARG106

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PDB entries from 2025-06-18

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