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4CVW

Structure of the barley limit dextrinase-limit dextrinase inhibitor complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0051060molecular_functionpullulanase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0051060molecular_functionpullulanase activity
C0004867molecular_functionserine-type endopeptidase inhibitor activity
C0005576cellular_componentextracellular region
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1885
ChainResidue
AGLN348
AASP351
ATYR353
AASN701

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 1886
ChainResidue
ASER297
ALEU301
AGLY393

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 1886
ChainResidue
BTYR353
BASN701
BGLN348
BASP351

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 1887
ChainResidue
BSER297
BLEU301
BGLY393

Functional Information from PROSITE/UniProt
site_idPS00426
Number of Residues24
DetailsCEREAL_TRYP_AMYL_INH Cereal trypsin/alpha-amylase inhibitors family signature. CqpgvDfphnPLatCHtYVikrvC
ChainResidueDetails
CCYS9-CYS32

222624

PDB entries from 2024-07-17

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