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3BRK

Crystal Structure of ADP-Glucose Pyrophosphorylase from Agrobacterium tumefaciens

Functional Information from GO Data
ChainGOidnamespacecontents
X0000166molecular_functionnucleotide binding
X0005524molecular_functionATP binding
X0005977biological_processglycogen metabolic process
X0005978biological_processglycogen biosynthetic process
X0008878molecular_functionglucose-1-phosphate adenylyltransferase activity
X0009058biological_processbiosynthetic process
X0016740molecular_functiontransferase activity
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 Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00624","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hv9
ChainResidueDetails
XARG25

249697

PDB entries from 2026-02-25

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