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1WDP

The role of an inner loop in the catalytic mechanism of soybean beta-amylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0005983biological_processstarch catabolic process
A0016161molecular_functionbeta-amylase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 2000
ChainResidue
AHIS146
AARG326
AARG330
AARG372
AHOH927
AHOH1146
AHOH1211
AHOH1274

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2001
ChainResidue
AARG130
AHOH988
AHOH1123
AHOH1173
AHIS119

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AALA222
AGLY225
ALYS304
ALYS453
AHOH1000
AHOH1052
AHOH1216
AHOH1265
AHOH1337

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
AARG347
ASER349
AHOH611
AHOH752
AHOH1186
AHOH1290
AHOH1326

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 2004
ChainResidue
AGLN77
AARG372
ATHR480
ALEU481
AHOH625
AHOH626
AHOH722
AHOH848
AHOH948
AHOH1076

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 2005
ChainResidue
ATHR256
AGLU257
ALYS428
AHOH610
AHOH916
AHOH958
AHOH1102
AHOH1111
AHOH1277

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 2006
ChainResidue
AASN98
APRO193
AGLN194
AHOH630
AHOH631
AHOH768
AHOH994
AHOH995
AHOH1029
AHOH1170

Functional Information from PROSITE/UniProt
site_idPS00506
Number of Residues9
DetailsBETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD
ChainResidueDetails
AHIS93-ASP101

site_idPS00679
Number of Residues11
DetailsBETA_AMYLASE_2 Beta-amylase active site 2. GpAGELRYPSY
ChainResidueDetails
AGLY182-TYR192

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2474529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8011643","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8174545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8011643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bya
ChainResidueDetails
AGLU186
AASP101

site_idMCSA1
Number of Residues5
DetailsM-CSA 436
ChainResidueDetails
AASP101electrostatic stabiliser
AGLU186proton shuttle (general acid/base)
ATHR342electrostatic stabiliser
AGLU380proton shuttle (general acid/base)
ALEU383steric role

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PDB entries from 2026-02-25

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