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2D3L

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0005983biological_processstarch catabolic process
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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP236
AGLU266
AASP333

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP236
AGLU266

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP236
AGLU266
ATRP268
AASP333

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU266
AASP236
AARG234
AHIS332
AASP333

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU266
AHIS107
AASP236
AASP333

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PDB entries from 2024-09-04

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