Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KP3

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0000053biological_processargininosuccinate metabolic process
A0004055molecular_functionargininosuccinate synthase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006526biological_processarginine biosynthetic process
A0016874molecular_functionligase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 456
ChainResidue
AGLU262
AARG269
AHOH595

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP A 457
ChainResidue
ATHR23
ATYR40
AALA42
AARG106
ALEU113
AASP127
AGLY128
ASER129
APHE139
AASP193
ACIR459
AHOH572
AHOH614
AHOH631
AALA16
APHE17
ASER18
AGLY20
ALEU21
AASP22

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CIR A 458
ChainResidue
ATYR98
ATHR102
APRO103
AASN134
AARG138
ASER191
AASP193
ATHR200
AGLU202
AGLU279
ATYR291
ACIR459

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIR A 459
ChainResidue
ATHR130
AGLY133
AASN134
AASP135
AGLU202
ASER287
AATP457
ACIR458
AHOH500

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GAI A 460
ChainResidue
AMET60
AALA64
AGLU65
AASN210
ASER211

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GAI A 461
ChainResidue
ATHR1
AASP399
AHOH584
AHOH609

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
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
AASP135
AARG106

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon