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1GAH

GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004339molecular_functionglucan 1,4-alpha-glucosidase activity
A0005975biological_processcarbohydrate metabolic process
A0005976biological_processpolysaccharide metabolic process
Functional Information from PDB Data
site_idSB1
Number of Residues7
DetailsBINDING SUBSITE FOR THE FIRST RESIDUE OF ACARBOSE
ChainResidue
AARG54
AASP55
ALEU177
AGLU179
AARG305
AGLU400
AHOH498

site_idSB2
Number of Residues4
DetailsBINDING SUBSITE FOR THE SECOND RESIDUE OF ACARBOSE
ChainResidue
AGLU179
AARG305
AGLU180
ATRP178

site_idSB3
Number of Residues2
DetailsBINDING SUBSITE FOR THE THIRD RESIDUE OF ACARBOSE
ChainResidue
AGLU179
AGLY121

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKSDGDELSarDL
ChainResidueDetails
AASP403-LEU415

site_idPS00820
Number of Residues11
DetailsGLUCOAMYLASE Glucoamylase active site region signature. TGy.DlWEEvnG
ChainResidueDetails
ATHR173-GLY183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10051
ChainResidueDetails
AASP176

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10051
ChainResidueDetails
AGLU179

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATRP120

site_idSWS_FT_FI4
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN171
AASN182
AASN395

site_idSWS_FT_FI5
Number of Residues6
DetailsCARBOHYD: O-linked (Man) serine => ECO:0000250
ChainResidueDetails
ASER441
ASER443
ASER459
ASER468
AALA442
AILE469

site_idSWS_FT_FI6
Number of Residues5
DetailsCARBOHYD: O-linked (Man) serine
ChainResidueDetails
ASER444
ASER460
AVAL445
AALA454
AVAL461

site_idSWS_FT_FI7
Number of Residues5
DetailsCARBOHYD: O-linked (Man) threonine => ECO:0000250
ChainResidueDetails
ATHR452
ATHR462
ATHR464
ATHR472

site_idSWS_FT_FI8
Number of Residues3
DetailsCARBOHYD: O-linked (Man) threonine
ChainResidueDetails
ASER453
ASER465
AVAL463

site_idSWS_FT_FI9
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10051, ECO:0000269|PubMed:1970434
ChainResidueDetails
ALEU177

site_idSWS_FT_FI10
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10051, ECO:0000269|PubMed:1970434
ChainResidueDetails
AGLU180

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLY121

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AGLN172
AGLY396

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1agm
ChainResidueDetails
AGLU179
AGLU400

site_idMCSA1
Number of Residues5
DetailsM-CSA 393
ChainResidueDetails
AGLY121transition state stabiliser
ALEU177proton shuttle (general acid/base), transition state stabiliser
AGLU180proton shuttle (general acid/base)
AVAL181activator
AGLN401activator

227344

PDB entries from 2024-11-13

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