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protein ligands metals links
Hydrolase PDB id
3blb
Jmol
Contents
Protein chain
1014 a.a. *
Ligands
NAG
SWA
MRD
Metals
_ZN
Waters ×1068
* Residue conservation analysis
PDB id:
3blb
Name: Hydrolase
Title: Crystal structure of golgi mannosidase ii in complex with sw at 1.3 angstrom resolution
Structure: Alpha-mannosidase 2. Chain: a. Fragment: catalytic domain: residues 76-1108. Synonym: alpha-mannosidase ii, mannosyl-oligosaccharide 1,3 alpha-mannosidase, man ii, golgi alpha-mannosidase ii, aman engineered: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Strain: berkeley. Tissue: head. Gene: alpha-man-ii, gmii, cg18802. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227.
Resolution:
1.30Å     R-factor:   0.166     R-free:   0.185
Authors: D.A.Kuntz,D.R.Rose
Key ref: D.A.Kuntz and d.r.rose Golgi mannosidase ii in complex with swainsonine at 1.3 angstrom.. To be published,
Date:
10-Dec-07     Release date:   08-Jan-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q24451  (MAN2_DROME) -  Alpha-mannosidase 2
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1108 a.a.
1014 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.114  - Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Mannosyl-glycoprotein N-acetylglucosaminyltransferases
      Reaction: Hydrolysis of the terminal 1,3- and 1,6-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man(5)(GlcNAc)(3).
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   6 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     11 terms