Structure of PDB 4aq0 Chain A

Receptor sequence
>4aq0A (length=765) Species: 1710 (Cellulosimicrobium cellulans) [Search protein sequence]
ADYASLVDVFVGTEGDFGNDMPAAQAPNGLAKVNPRTTPGRNNTGYDYAQ
SKISGFTHTNLDGVGGSGGGGDLLVVPTSGSYTARPGTGTYAHPFSHDDE
DAGPGFYSVGLGNVAGTDGAITGAPGTIEAEVAAATRSGVHRYAFPAGST
PSLVVDLETNNTSRRSSSVQVETRADGTVELSGQVTGYFYNAAYTLYYTA
RTLQPATVQTWGDDDRLVDATAQDGVDTGAILTFDPADAGEIGLQVTLSP
VSVEQARIDQQVELGDLSFDAIRDRTRAEWNATLGRVAIDASTATDPTGE
LQRLFYTHLYRMFAMPMNATSTSGTYRGVDGAVHAAQGFTYYDSWATWDD
FRKFSVIAYIDPALYRDMVQSLVYLFADAEATGTGGGLGGFVHSVPTVRW
ERSSVVVADAIAKGFDGFDRLDEAYPALQRLVGQYSADELRRGYVAGNPG
ASVQRGYDQYGLSVIADELGLTEEAETLREQASWPIEKLTKPGAWTAADG
TQVGLLTPRAADGSWQSADHAKFEAAGLYQGTLWQYHWYDAYDMDALVEA
MGGHEAARLGMRHMFGEHAPDDGKAMLHSNANEIDLQAPYLFNYTGEPSL
TQKWARAIYTKETWNRYIATGSSSAVPSGGGEFTPPLKTKVYRLDPRGML
PTMDNDAGTMSTMFVAAAVGLFPVTAGSSQFQVGSPFFDSTTITYDDGSA
FTVTADGVSEDAFYVQSATLDGATFGNTWVDYATVVGGADLAFRMGEQPS
DWGTDTAPAFSMSTA
3D structure
PDB4aq0 A Bacterial Glycosidase Enables Mannose-6-Phosphate Modification and Improved Cellular Uptake of Yeast-Produced Recombinant Human Lysosomal Enzymes.
ChainA
Resolution2.09 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.24: alpha-mannosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A N588 E589 D662 N582 E583 D656
Gene Ontology
Molecular Function
GO:0000224 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity
GO:0004559 alpha-mannosidase activity
GO:0030246 carbohydrate binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
GO:0006516 glycoprotein catabolic process
GO:0006517 protein deglycosylation
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4aq0, PDBe:4aq0, PDBj:4aq0
PDBsum4aq0
PubMed23159880
UniProtM1E1E9

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