Structure of PDB 3gly Chain A

Receptor sequence
>3glyA (length=470) Species: 105351 (Aspergillus awamori) [Search protein sequence]
ATLDSWLSNEATVARTAILNNIGADGAWVSGADSGIVVASPSTDNPDYFY
TWTRDSGLVIKTLVDLFRNGDTDLLSTIEHYISSQAIIQGVSNPSGDLSS
GGLGEPKFNVDETAYTGSWGRPQRDGPALRATAMIGFGQWLLDNGYTSAA
TEIVWPLVRNDLSYVAQYWNQTGYDLWEEVNGSSFFTIAVQHRALVEGSA
FATAVGSSCSWCDSQAPQILCYLQSFWTGSYILANFDSSRSGKDTNTLLG
SIHTFDPEAGCDDSTFQPCSPRALANHKEVVDSFRSIYTLNDGLSDSEAV
AVGRYPEDSYYNGNPWFLCTLAAAEQLYDALYQWDKQGSLEITDVSLDFF
KALYSGAATGTYSSSSSTYSSIVSAVKTFADGFVSIVETHAASNGSLSEQ
FDKSDGDELSARDLTWSYAALLTANNRRNSVVPPSWGETSASSVPGTCAA
TSASGTYSSVTVTSWPSIVA
3D structure
PDB3gly Refined crystal structures of glucoamylase from Aspergillus awamori var. X100.
ChainA
Resolution2.2 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
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MAN A F237 D238 S239 F236 D237 S238
BS02 MAN A S30 P41 F49 S30 P41 F49
BS03 MAN A S42 S411 R413 S42 S410 R412
BS04 MAN A E439 T440 S441 S443 S444 E438 T439 S440 S442 S443
BS05 MAN A T452 S453 T451 S452
BS06 MAN A R160 S459 S460 R159 S458 S459
BS07 MAN A A86 G90 S460 A86 G90 S459
BS08 MAN A S460 T462 S459 T461
BS09 MAN A T462 T464 T461 T463
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:3gly, PDBe:3gly, PDBj:3gly
PDBsum3gly
PubMed8176747
UniProtP69327|AMYG_ASPAW Glucoamylase (Gene Name=GLAA)

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