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1LOO

Crystal Structure of the Mouse-Muscle Adenylosuccinate Synthetase Ligated with GTP

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
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GTP A 458
ChainResidue
AASP43
AGLY447
ALYS448
AHOH509
AHOH530
AHOH533
AHOH536
AHOH562
AHOH597
AGLY45
ALYS46
ALYS48
ALYS363
AASP365
AILE366
AGLY445
AVAL446

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03126
ChainResidueDetails
AASP43

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_03126
ChainResidueDetails
AHIS71

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:12004071
ChainResidueDetails
AARG177
AARG337
ALYS363
AGLY445
AGLY42

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AASP43
AGLY70
AVAL331

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: in other chain
ChainResidueDetails
AASN68

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:12004071
ChainResidueDetails
AASN256
ATHR271
AARG335
ATHR163

221051

PDB entries from 2024-06-12

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