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1IWE

IMP Complex of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003924molecular_functionGTPase activity
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
A0006531biological_processaspartate metabolic process
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0042802molecular_functionidentical protein binding
A0044208biological_process'de novo' AMP biosynthetic process
A0044209biological_processAMP salvage
A0046040biological_processIMP metabolic process
A0046872molecular_functionmetal ion binding
A0051015molecular_functionactin filament binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003924molecular_functionGTPase activity
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
B0006531biological_processaspartate metabolic process
B0016020cellular_componentmembrane
B0016874molecular_functionligase activity
B0042802molecular_functionidentical protein binding
B0044208biological_process'de novo' AMP biosynthetic process
B0044209biological_processAMP salvage
B0046040biological_processIMP metabolic process
B0046872molecular_functionmetal ion binding
B0051015molecular_functionactin filament binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1442
ChainResidue
BGLY70
BHOH575
BHOH903
BHOH904
BHOH936
BIMP1452

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 458
ChainResidue
ALYS46
AHIS71
AHOH774
AHOH855
AASP43
AGLU44
AGLY45

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 459
ChainResidue
AGLY330
AVAL331
ATHR332
ATHR333
AARG335
AIMP460

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE IMP B 1443
ChainResidue
AARG177
BTRP41
BASP43
BASN68
BILE160
BGLY161
BTHR162
BTHR163
BILE167
BPHE269
BVAL270
BTHR271
BVAL305
BHOH563
BHOH693
BHOH719
BHOH832
BHOH861

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE IMP B 1452
ChainResidue
BGLU44
BGLY45
BLYS46
BGLY47
BLYS48
BGLY70
BHIS71
BTHR72
BLYS363
BASP365
BGLY445
BVAL446
BGLY447
BLYS448
BHOH555
BHOH620
BHOH627
BHOH724
BHOH936
BMG1442

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE IMP A 460
ChainResidue
AASP43
AASN68
AALA69
AILE160
AGLY161
ATHR162
ATHR163
AASN256
ALEU260
AVAL270
ATHR271
AVAL305
AARG335
AACT459
AHOH507
AHOH529
AHOH538
AHOH547
AHOH588
AHOH774
BARG177

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

223166

PDB entries from 2024-07-31

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