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3BRK

Crystal Structure of ADP-Glucose Pyrophosphorylase from Agrobacterium tumefaciens

Functional Information from GO Data
ChainGOidnamespacecontents
X0005524molecular_functionATP binding
X0005978biological_processglycogen biosynthetic process
X0008878molecular_functionglucose-1-phosphate adenylyltransferase activity
X0009058biological_processbiosynthetic process
X0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 600
ChainResidue
XSER334
XASN350
XSER351
XARG368
XHOH712
XHOH812

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 X 602
ChainResidue
XARG318
XARG368

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 X 601
ChainResidue
XTYR39
XARG45
XSER72
XARG33

Functional Information from PROSITE/UniProt
site_idPS00808
Number of Residues20
DetailsADP_GLC_PYROPHOSPH_1 ADP-glucose pyrophosphorylase signature 1. AGGrGSrLkeLTdrrAkPAV
ChainResidueDetails
XALA19-VAL38

site_idPS00809
Number of Residues9
DetailsADP_GLC_PYROPHOSPH_2 ADP-glucose pyrophosphorylase signature 2. WYeGTADAV
ChainResidueDetails
XTRP106-VAL114

site_idPS00810
Number of Residues11
DetailsADP_GLC_PYROPHOSPH_3 ADP-glucose pyrophosphorylase signature 3. ASMGIYVFhtK
ChainResidueDetails
XALA204-LYS214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00624
ChainResidueDetails
XTYR107
XGLY172
XGLU187
XSER205

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PDB entries from 2024-06-12

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