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3HID

Crystal structure of adenylosuccinate synthetase from Yersinia pestis CO92

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 Residues2
DetailsBINDING SITE FOR RESIDUE PG6 A 433
ChainResidue
ATYR176
ATYR177

Functional Information from PROSITE/UniProt
site_idPS00513
Number of Residues12
DetailsADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPaYedKvaR
ChainResidueDetails
AGLY133-ARG144

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AASP14

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AHIS42

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AGLY13
AASP14
AGLY41
AARG144
AALA300
AARG306
ALYS332
ASER415

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AASN39
ATHR130
AGLN225
ATHR240
AARG304

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gim
ChainResidueDetails
AHIS42
AGLN225
AASP14

225946

PDB entries from 2024-10-09

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