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3UE9

Crystal structure of Adenylosuccinate synthetase (AMPSase) (purA) from Burkholderia thailandensis

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
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004019molecular_functionadenylosuccinate synthase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0006164biological_processpurine nucleotide biosynthetic process
B0016874molecular_functionligase activity
B0044208biological_process'de novo' AMP biosynthetic process
B0046040biological_processIMP metabolic process
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0004019molecular_functionadenylosuccinate synthase activity
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0006164biological_processpurine nucleotide biosynthetic process
C0016874molecular_functionligase activity
C0044208biological_process'de novo' AMP biosynthetic process
C0046040biological_processIMP metabolic process
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0004019molecular_functionadenylosuccinate synthase activity
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0006164biological_processpurine nucleotide biosynthetic process
D0016874molecular_functionligase activity
D0044208biological_process'de novo' AMP biosynthetic process
D0046040biological_processIMP metabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 449
ChainResidue
APRO209
AHOH471
AHOH794
AHOH795
AHOH854
AHOH855

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 449
ChainResidue
BHOH511
BHOH761
BHOH875
BPRO209
BHOH455
BHOH472

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 449
ChainResidue
APHE177
CARG127
CLEU186
CHOH684

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA C 450
ChainResidue
CPRO209
CHOH600
CHOH663
CHOH772
CHOH773
CHOH774
CHOH823

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT D 449
ChainResidue
BARG154
DARG127

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA D 450
ChainResidue
DPRO209
DHOH534
DHOH569
DHOH791
DHOH792
DHOH793
DHOH1128

Functional Information from PROSITE/UniProt
site_idPS00513
Number of Residues12
DetailsADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPaYedKvgR
ChainResidueDetails
AGLY142-ARG153

site_idPS01266
Number of Residues8
DetailsADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG
ChainResidueDetails
AGLN20-GLY27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues85
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues33
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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