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1BFN

BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0008152biological_processmetabolic process
A0016161molecular_functionbeta-amylase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0102229molecular_functionamylopectin maltohydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00506
Number of Residues9
DetailsBETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD
ChainResidueDetails
AHIS93-ASP101

site_idPS00679
Number of Residues11
DetailsBETA_AMYLASE_2 Beta-amylase active site 2. GpAGELRYPSY
ChainResidueDetails
AGLY182-TYR192

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10050, ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:2474529, ECO:0000269|PubMed:8011643, ECO:0000269|PubMed:8174545
ChainResidueDetails
ALEU187

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:8011643
ChainResidueDetails
AASN381

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15178253
ChainResidueDetails
ALEU421
AVAL54
AGLN94
AILE102
AVAL296
ATRP301
ACYS343
AALA382

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:2430952
ChainResidueDetails
ATHR2

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 436
ChainResidueDetails
AILE102electrostatic stabiliser
ALEU187proton shuttle (general acid/base)
ACYS343electrostatic stabiliser
AASN381proton shuttle (general acid/base)
APRO384steric role

218500

PDB entries from 2024-04-17

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