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2XFR

Crystal structure of barley beta-amylase at atomic resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0016161molecular_functionbeta-amylase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042802molecular_functionidentical protein binding
A0102229molecular_functionamylopectin maltohydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1490
ChainResidue
ATHR127
AASN129
APRO188
APRO191
ATYR236
AHOH2492
AHOH2943

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1491
ChainResidue
AGLU228
APHE229
AHOH2945
AHOH2947
AHOH2948
AGLN212
APHE215

Functional Information from PROSITE/UniProt
site_idPS00506
Number of Residues9
DetailsBETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD
ChainResidueDetails
AHIS91-ASP99

site_idPS00679
Number of Residues11
DetailsBETA_AMYLASE_2 Beta-amylase active site 2. GpAGEMRYPSY
ChainResidueDetails
AGLY180-TYR190

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10050
ChainResidueDetails
AGLU184

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P10538
ChainResidueDetails
AGLU378

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P10538
ChainResidueDetails
AASP51
AHIS91
AASP99
ALYS293
AHIS298
ATHR340
AASN379
AARG418

225158

PDB entries from 2024-09-18

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