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3R7T

Crystal Structure of Adenylosuccinate Synthetase from Campylobacter jejuni

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004019molecular_functionadenylosuccinate synthase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0016874molecular_functionligase activity
A0044208biological_process'de novo' AMP biosynthetic process
A0046040biological_processIMP metabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT A 421
ChainResidue
AVAL269
AHOH595
AGLY294
AVAL295
ASER296
ATHR297
AARG301
AHOH491
AHOH542
AHOH568

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE A 422
ChainResidue
ALYS285
AASP332
AGLY333
APHE334
AHOH545
AHOH651

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGE A 423
ChainResidue
AASP98
ALEU149
AILE197
ATYR345
ALYS346
AASP356
AHOH486

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 424
ChainResidue
AHIS143
AGLU147
AHOH621
AHOH628

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 425
ChainResidue
ATYR95
ATHR198
AHOH627

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 426
ChainResidue
ALEU149
ALYS187
AASN190

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 427
ChainResidue
AGLU88

Functional Information from PROSITE/UniProt
site_idPS00513
Number of Residues12
DetailsADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPsYadKinR
ChainResidueDetails
AGLY129-ARG140

site_idPS01266
Number of Residues8
DetailsADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG
ChainResidueDetails
AGLN11-GLY18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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