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2GUY

Orthorhombic crystal structure (space group P21212) of Aspergillus niger alpha-amylase at 1.6 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0009277cellular_componentfungal-type cell wall
A0016052biological_processcarbohydrate catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030287cellular_componentcell wall-bounded periplasmic space
A0030428cellular_componentcell septum
A0031521cellular_componentspitzenkorper
A0032163cellular_componenthyphal septin band
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:9283074
ChainResidueDetails
AASP206

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:9283074
ChainResidueDetails
AGLU230

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:9283074
ChainResidueDetails
AHIS122
AARG204
ALYS209
AGLY234
AASP297
AARG344
AGLN35
ATRP83

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074
ChainResidueDetails
AASP175
AHIS210
AASN121
AGLU162

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:9283074
ChainResidueDetails
AGLU230
AASP206

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:9283074
ChainResidueDetails
AASP297

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16880540
ChainResidueDetails
AASN197

219869

PDB entries from 2024-05-15

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