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6FRV

Structure of the catalytic domain of Aspergillus niger Glucoamylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0003824molecular_functioncatalytic activity
A0004339molecular_functionglucan 1,4-alpha-glucosidase activity
A0005783cellular_componentendoplasmic reticulum
A0005975biological_processcarbohydrate metabolic process
A0005976biological_processpolysaccharide metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A2001070molecular_functionstarch binding
Functional Information from PROSITE/UniProt
site_idPS00820
Number of Residues11
DetailsGLUCOAMYLASE Glucoamylase active site region signature. TGy.DlWEEvnG
ChainResidueDetails
ATHR197-GLY207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10051
ChainResidueDetails
AASP200

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10051
ChainResidueDetails
AGLU203

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATRP144

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250
ChainResidueDetails
AASN195
AASN419

site_idSWS_FT_FI5
Number of Residues18
DetailsCARBOHYD: O-linked (Man) serine => ECO:0000269|Ref.4
ChainResidueDetails
ASER465
ASER510
ASER513
ASER515
ASER522
ASER525
ASER527
ASER529
ASER530
ASER532
ASER467
ASER468
ASER477
ASER483
ASER484
ASER489
ASER492
ASER508

site_idSWS_FT_FI6
Number of Residues21
DetailsCARBOHYD: O-linked (Man) threonine => ECO:0000269|Ref.4
ChainResidueDetails
ATHR476
ATHR506
ATHR512
ATHR514
ATHR517
ATHR518
ATHR520
ATHR524
ATHR526
ATHR528
ATHR531
ATHR486
ATHR534
ATHR535
ATHR488
ATHR496
ATHR499
ATHR500
ATHR501
ATHR502
ATHR504

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PDB entries from 2024-07-24

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