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2D3N

Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005975biological_processcarbohydrate metabolic process
A0005983biological_processstarch catabolic process
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033927molecular_functionglucan 1,4-alpha-maltohexaosidase activity
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP236

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU266

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00692
ChainResidueDetails
AASN106
AASP163
AALA186
AASP188
AASP199
AASP205
AASP207
AASP209
AHIS240

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP333

218853

PDB entries from 2024-04-24

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