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6XSJ

X-ray structure of a monoclinic form of alpha amylase from Aspergillus at 1.4 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005975biological_processcarbohydrate metabolic process
A0016052biological_processcarbohydrate catabolic process
A0043169molecular_functioncation binding
B0004556molecular_functionalpha-amylase activity
B0005509molecular_functioncalcium ion binding
B0005975biological_processcarbohydrate metabolic process
B0016052biological_processcarbohydrate catabolic process
B0043169molecular_functioncation binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:9283074
ChainResidueDetails
AASP206
BASP206

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:9283074
ChainResidueDetails
AGLU230
BGLU230

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000305|PubMed:9283074
ChainResidueDetails
AGLN35
BTRP83
BHIS122
BARG204
BLYS209
BGLY234
BASP297
BARG344
ATRP83
AHIS122
AARG204
ALYS209
AGLY234
AASP297
AARG344
BGLN35

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074
ChainResidueDetails
AASN121
AGLU162
AASP175
AHIS210
BASN121
BGLU162
BASP175
BHIS210

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9283074
ChainResidueDetails
AASP206
AGLU230
BASP206
BGLU230

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:9283074
ChainResidueDetails
AASP297
BASP297

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16880540
ChainResidueDetails
AASN197
BASN197

220113

PDB entries from 2024-05-22

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