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1MEZ

Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with SAMP, GDP, SO4(2-), and Mg(2+)

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1453
ChainResidue
AASP43
AGLY70
AGDP1452
ASO41454
A2SA1455

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 1454
ChainResidue
AGLY70
AHIS71
AALA255
AASN256
AGDP1452
AMG1453
A2SA1455
AGLY42
AASP43
ALYS46
AALA69

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP A 1452
ChainResidue
AASP43
AGLU44
AGLY45
ALYS46
AGLY47
ALYS48
AGLY70
AHIS71
ATHR72
AVAL331
AARG337
ALYS363
AASP365
AILE366
AGLY445
AVAL446
AGLY447
ALYS448
AHOH504
AHOH529
AHOH553
AMG1453
ASO41454
A2SA1455

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 2SA A 1455
ChainResidue
ATRP41
AASP43
AASN68
AGLY70
ATHR162
ATHR163
AARG177
AASN256
ALEU260
AVAL270
ATHR271
AVAL305
AGLY330
AVAL331
ATHR332
ATHR333
AARG335
AARG337
AHOH515
AHOH532
AHOH559
AHOH613
AGDP1452
AMG1453
ASO41454

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
AGLY42
AARG177
AARG337
ALYS363
AGLY445

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
ATHR163
AASN256
ATHR271
AARG335

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PDB entries from 2024-11-13

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