Structure of PDB 1gah Chain A

Receptor sequence
>1gahA (length=471) Species: 105351 (Aspergillus awamori) [Search protein sequence]
ATLDSWLSNEATVARTAILNNIGADGAWVSGADSGIVVASPSTDNPDYFY
TWTRDSGLVIKTLVDLFRNGDTDLLSTIEHYISSQAIIQGVSNPSGDLSS
GGLGEPKFNVDETAYTGSWGRPQRDGPALRATAMIGFGQWLLDNGYTSAA
TEIVWPLVRNDLSYVAQYWNQTGYDLWEEVNGSSFFTIAVQHRALVEGSA
FATAVGSSCSWCDSQAPQILCYLQSFWTGSYILANFDSSRSGKDTNTLLG
SIHTFDPEAGCDDSTFQPCSPRALANHKEVVDSFRSIYTLNDGLSDSEAV
AVGRYPEDSYYNGNPWFLCTLAAAEQLYDALYQWDKQGSLEITDVSLDFF
KALYSGAATGTYSSSSSTYSSIVSAVKTFADGFVSIVETHAASNGSLSEQ
FDKSDGDELSARDLTWSYAALLTANNRRNSVVPPSWGETSASSVPGTCAA
TSASGTYSSVTVTSWPSIVAT
3D structure
PDB1gah Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W120 D176 E179 E180 E400
Catalytic site (residue number reindexed from 1) W119 D175 E178 E179 E399
Enzyme Commision number 3.2.1.3: glucan 1,4-alpha-glucosidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004339 glucan 1,4-alpha-glucosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005976 polysaccharide metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1gah, PDBe:1gah, PDBj:1gah
PDBsum1gah
PubMed8679589
UniProtP69327|AMYG_ASPAW Glucoamylase (Gene Name=GLAA)

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