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1KJX

IMP Complex of E. Coli Adenylosuccinate Synthetase

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
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006974biological_processDNA damage response
A0015949biological_processnucleobase-containing small molecule interconversion
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0044208biological_process'de novo' AMP biosynthetic process
A0046040biological_processIMP metabolic process
A0046086biological_processadenosine biosynthetic process
A0046872molecular_functionmetal ion binding
A0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE IMP A 440
ChainResidue
AASP13
ATHR239
AVAL273
AGLY274
AARG303
AHOH483
AHOH562
AASN38
AGLY127
ATHR128
ATHR129
AARG143
AGLN224
ALEU228
AVAL238

Functional Information from PROSITE/UniProt
site_idPS00513
Number of Residues12
DetailsADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPaYedKvaR
ChainResidueDetails
AGLY132-ARG143

site_idPS01266
Number of Residues8
DetailsADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG
ChainResidueDetails
AGLN10-GLY17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP13

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS41

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011, ECO:0000269|PubMed:10346917
ChainResidueDetails
AGLY12
AARG305
ALYS331
ASER414

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011, ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:8961938, ECO:0000269|PubMed:9000627
ChainResidueDetails
AASP13
AGLY40

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: in other chain
ChainResidueDetails
AASN38

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00011, ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627
ChainResidueDetails
ATHR129
AGLN224
ATHR239
AARG303

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011, ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627
ChainResidueDetails
AARG143

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AALA299

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gim
ChainResidueDetails
AASP13
AGLN224
AHIS41

site_idMCSA1
Number of Residues5
DetailsM-CSA 65
ChainResidueDetails
AASP13electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
ALYS16electrostatic stabiliser, hydrogen bond donor
AGLY40metal ligand
AHIS41electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLN224electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-08-14

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