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

1LNY

Crystal structure of the recombinant mouse-muscle adenylosuccinate synthetase complexed with 6-phosphoryl-IMP, GDP and Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004019molecular_functionadenylosuccinate synthase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0006163biological_processpurine nucleotide metabolic process
A0006164biological_processpurine nucleotide biosynthetic process
A0006167biological_processAMP biosynthetic process
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0044208biological_process'de novo' AMP biosynthetic process
A0044209biological_processAMP salvage
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004019molecular_functionadenylosuccinate synthase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0006163biological_processpurine nucleotide metabolic process
B0006164biological_processpurine nucleotide biosynthetic process
B0006167biological_processAMP biosynthetic process
B0016020cellular_componentmembrane
B0016874molecular_functionligase activity
B0044208biological_process'de novo' AMP biosynthetic process
B0044209biological_processAMP salvage
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1453
ChainResidue
AASP43
AGLY70
AHOH817
AIMO1451
AGDP1452

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1456
ChainResidue
BIMO1455
BASP43
BGLY70
BHOH696
BGDP1454

site_idAC3
Number of Residues27
DetailsBINDING SITE FOR RESIDUE IMO A 1451
ChainResidue
ATRP41
AGLY42
AASP43
ALYS46
AASN68
AALA69
AGLY70
AHIS71
AGLY161
ATHR162
ATHR163
AASN256
ALEU260
AVAL270
ATHR271
AVAL305
AGLY306
AARG335
AHOH501
AHOH602
AHOH649
AHOH660
AHOH703
AHOH817
AGDP1452
AMG1453
BARG177

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP A 1452
ChainResidue
AASP43
AGLU44
AGLY45
ALYS46
AGLY47
ALYS48
AGLY70
AHIS71
ATHR72
ALYS363
AASP365
AGLY445
AVAL446
AGLY447
ALYS448
AHOH581
AHOH645
AHOH817
AIMO1451
AMG1453

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP B 1454
ChainResidue
BASP43
BGLU44
BGLY45
BLYS46
BGLY47
BLYS48
BGLY70
BHIS71
BTHR72
BLYS363
BASP365
BGLY445
BVAL446
BGLY447
BLYS448
BHOH594
BHOH710
BIMO1455
BMG1456

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE IMO B 1455
ChainResidue
BMG1456
AARG177
BTRP41
BGLY42
BASP43
BLYS46
BASN68
BALA69
BGLY70
BHIS71
BGLY161
BTHR162
BTHR163
BASN256
BLEU260
BVAL270
BTHR271
BVAL305
BGLY306
BHOH514
BHOH534
BHOH577
BHOH659
BGDP1454

Functional Information from PROSITE/UniProt
site_idPS00513
Number of Residues12
DetailsADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPtYssKaaR
ChainResidueDetails
AGLY166-ARG177

site_idPS01266
Number of Residues8
DetailsADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG
ChainResidueDetails
AGLN40-GLY47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03126
ChainResidueDetails
AASP43
BASP43

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_03126
ChainResidueDetails
AHIS71
BHIS71

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:12004071
ChainResidueDetails
AGLY42
BGLY445
AARG177
AARG337
ALYS363
AGLY445
BGLY42
BARG177
BARG337
BLYS363

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP43
AGLY70
AVAL331
BASP43
BGLY70
BVAL331

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: in other chain
ChainResidueDetails
AASN68
BASN68

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:12004071
ChainResidueDetails
ATHR163
AASN256
ATHR271
AARG335
BTHR163
BASN256
BTHR271
BARG335

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon