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3GLY

REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100

Replaces:  1GLY
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_idACT
Number of Residues4
DetailsACTIVE SITE: RESIDUES THAT BIND ACARBOSE AND 1-DEOXYNOJIRIMYCIN AT SUBSITE 1 OF THE ACTIVE SITE ARE OD1 ASP 55, OD2 ASP 55, NH1 ARG 305, CARBONYL 177, NE ARG 54, AND NH2 ARG 54. GLU 179 IS THE CATALYTIC ACID AND RESIDUE GLU 400 IS THE CATALYTIC BASE. WATER 500 IS THE NUCLEOPHILE.
ChainResidue
AASP55
AARG305
ALEU177
AARG54

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 Residues3
DetailsCARBOHYD: O-linked (Man) threonine => ECO:0000250
ChainResidueDetails
ATHR452
ATHR462
ATHR464

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

225946

PDB entries from 2024-10-09

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