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2QLY

Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030246molecular_functioncarbohydrate binding
Functional Information from PROSITE/UniProt
site_idPS00025
Number of Residues22
DetailsP_TREFOIL_1 P-type 'Trefoil' domain signature. RinCiPdqppTkatCdqrgCCW
ChainResidueDetails
AARG12-TRP33

site_idPS00129
Number of Residues8
DetailsGLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. GIWiDMNE
ChainResidueDetails
AGLY439-GLU446

site_idPS00707
Number of Residues31
DetailsGLYCOSYL_HYDROL_F31_2 Glycosyl hydrolases family 31 signature 2. GPDICGFaldTpeeLCrRWmqLGAFyPFsRN
ChainResidueDetails
AGLY569-ASN599

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10066
ChainResidueDetails
AASP443

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AGLU446

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18036614
ChainResidueDetails
AASP203
AASP327
AARG526
AASP542
AHIS600

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Sulfotyrosine => ECO:0000255
ChainResidueDetails
ATYR330
ATYR339

site_idSWS_FT_FI5
Number of Residues7
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN49
AASN371
AASN372
AASN621
AASN663
AASN799
AASN826

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18036614
ChainResidueDetails
AASN209
AASN393
AASN741

219140

PDB entries from 2024-05-01

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