Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1UA7

Crystal Structure Analysis of Alpha-Amylase from Bacillus Subtilis complexed with Acarbose

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005975biological_processcarbohydrate metabolic process
A0043169molecular_functioncation binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:9514750
ChainResidueDetails
AASP176

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:9514750
ChainResidueDetails
AGLU208

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:9514750
ChainResidueDetails
AASN101
ATHR137
AASP146
AGLY169
AASP171
AHIS180

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:9514750
ChainResidueDetails
AASP269

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU208
AASP176

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU208
AHIS268
AASP269
AARG174
AASP176

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AHIS102
AGLU208
AASP269
AASP176

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP269
AGLU208
AASP176

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon