Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6B9O

Structure of GH 38 Jack Bean alpha-mannosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000326cellular_componentprotein storage vacuole
A0003824molecular_functioncatalytic activity
A0004559molecular_functionalpha-mannosidase activity
A0005773cellular_componentvacuole
A0005975biological_processcarbohydrate metabolic process
A0006013biological_processmannose metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0046872molecular_functionmetal ion binding
B0000326cellular_componentprotein storage vacuole
B0003824molecular_functioncatalytic activity
B0004559molecular_functionalpha-mannosidase activity
B0005773cellular_componentvacuole
B0005975biological_processcarbohydrate metabolic process
B0006013biological_processmannose metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9442045
ChainResidueDetails
AASP145
BASP145

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q29451
ChainResidueDetails
AHIS23
AASP25
AASP145
AHIS386
BHIS23
BASP25
BASP145
BHIS386

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; to produce subunits => ECO:0000269|PubMed:24295789
ChainResidueDetails
ATHR562
BTHR562

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:24295789
ChainResidueDetails
AASN312
AASN446
BASN312
BASN446

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon