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8J5D

Cryo-EM structure of starch degradation complex of BAM1-LSF1-MDH

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0016161molecular_functionbeta-amylase activity
B0003824molecular_functioncatalytic activity
B0006099biological_processtricarboxylic acid cycle
B0006108biological_processmalate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016615molecular_functionmalate dehydrogenase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0030060molecular_functionL-malate dehydrogenase activity
C0003824molecular_functioncatalytic activity
C0006099biological_processtricarboxylic acid cycle
C0006108biological_processmalate metabolic process
C0016491molecular_functionoxidoreductase activity
C0016615molecular_functionmalate dehydrogenase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019752biological_processcarboxylic acid metabolic process
C0030060molecular_functionL-malate dehydrogenase activity
D0006470biological_processprotein dephosphorylation
D0016311biological_processdephosphorylation
D0019203molecular_functioncarbohydrate phosphatase activity
Functional Information from PROSITE/UniProt
site_idPS00068
Number of Residues13
DetailsMDH Malate dehydrogenase active site signature. VTTLDvvRAntfV
ChainResidueDetails
BVAL227-VAL239

site_idPS00506
Number of Residues9
DetailsBETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD
ChainResidueDetails
AHIS187-ASP195

site_idPS00679
Number of Residues11
DetailsBETA_AMYLASE_2 Beta-amylase active site 2. GpAGELRYPSY
ChainResidueDetails
AGLY275-TYR285

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160
ChainResidueDetails
DCYS390
CHIS258

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
DCYS390
CMET309
BASP115
BASN175
BILE198
BMET309
CGLY89
CASP115
CASN175
CILE198

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P11708
ChainResidueDetails
BARG162
BARG168
BASN200
BARG234
CARG162
CARG168
CASN200
CARG234

220113

PDB entries from 2024-05-22

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