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1GA7

CRYSTAL STRUCTURE OF THE ADP-RIBOSE PYROPHOSPHATASE IN COMPLEX WITH GD+3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006753biological_processnucleoside phosphate metabolic process
A0009408biological_processresponse to heat
A0016462molecular_functionpyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0016818molecular_functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
A0019144molecular_functionADP-sugar diphosphatase activity
A0019693biological_processribose phosphate metabolic process
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0047631molecular_functionADP-ribose diphosphatase activity
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006753biological_processnucleoside phosphate metabolic process
B0009408biological_processresponse to heat
B0016462molecular_functionpyrophosphatase activity
B0016787molecular_functionhydrolase activity
B0016818molecular_functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
B0019144molecular_functionADP-sugar diphosphatase activity
B0019693biological_processribose phosphate metabolic process
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0047631molecular_functionADP-ribose diphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GD3 A 302
ChainResidue
AARG35
AGLU48
AGLU112
AGLU115

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GD3 B 301
ChainResidue
BGLU112
BGLU115
BGLU164
BHOH304
BHOH305

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GmieegEsvedVArREAiEEaG
ChainResidueDetails
AGLY97-GLY118

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AGLU162
BGLU162

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: in other chain
ChainResidueDetails
APHE28
BGLU139
AARG56
AARG79
AMET98
AGLU139
BPHE28
BARG56
BARG79
BMET98

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AARG51
BGLU116
BSER133
BGLU164
AALA96
AGLU112
AGLU116
ASER133
AGLU164
BARG51
BALA96
BGLU112

224004

PDB entries from 2024-08-21

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