Structure of PDB 3eqa Chain A

Receptor sequence
>3eqaA (length=458) Species: 5061 (Aspergillus niger) [Search protein sequence]
WLSNEATVARTAILNNIGADGAWVSGADSGIVVASPSTDNPDYFYTWTRD
SGLVLKTLVDLFRNGDTSLLSTIENYISAQAIVQGISNPSGDLSSGAGLG
EPKFNVDETAYTGSWGRPQRDGPALRATAMIGFGQWLLDNGYTSTATDIV
WPLVRNDLSYVAQYWNQTGYDLWEEVNGSSFFTIAVQHRALVEGSAFATA
VGSSCSWCDSQAPEILCYLQSFWTGSFILANFDSSRSGKDANTLLGSIHT
FDPEAACDDSTFQPCSPRALANHKEVVDSFRSIYTLNDGLSDSEAVAVGR
YPEDTYYNGNPWFLCTLAAAEQLYDALYQWDKQGSLEVTDVSLDFFKALY
SDAATGTYSSSSSTYSSIVDAVKTFADGFVSIVETHAASNGSMSEQYDKS
DGEQLSARDLTWSYAALLTANNRRNSVVPASWGETSASSVPGTCAATSAI
GTYSSVTV
3D structure
PDB3eqa Structure of the catalytic domain of glucoamylase from Aspergillus niger.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W144 D200 E203 E204 E424
Catalytic site (residue number reindexed from 1) W115 D171 E174 E175 E395
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 S54 P65 S25 P36
BS02 MAN A S66 S435 R437 S37 S406 R408
BS03 MAN A E463 T464 S465 A466 S467 S468 E434 T435 S436 A437 S438 S439
BS04 MAN A S468 P470 S439 P441
BS05 MAN A T476 S477 T447 S448
BS06 MAN A S483 S484 S454 S455
BS07 MAN A A110 I111 G114 S484 A81 I82 G85 S455
BS08 MAN A S484 T486 S455 T457
BS09 GOL A W202 E204 W173 E175
Gene Ontology
Molecular Function
GO:0004339 glucan 1,4-alpha-glucosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005976 polysaccharide metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3eqa, PDBe:3eqa, PDBj:3eqa
PDBsum3eqa
PubMed21301084
UniProtP69328|AMYG_ASPNG Glucoamylase (Gene Name=GLAA)

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