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protein ligands metals links
Hydrolase PDB id
3bvx
Jmol
Contents
Protein chain
1016 a.a. *
Ligands
WZ5
MPD
Metals
_ZN
Waters ×1526
* Residue conservation analysis
PDB id:
3bvx
Name: Hydrolase
Title: Golgi mannosidase ii d204a catalytic nucleophile mutant complex with methyl (2-deoxy-2-acetamido-beta-d- glucopyranosyl)-(1->2)-(alpha-d-mannopyranosyl)- (1->3)- [(alpha-d-mannopyranosyl)-(1->6)-(alpha-d-mannopyranosyl)- (1->6)]-beta-d-mannopyranoside
Structure: Alpha-mannosidase 2. Chain: a. Fragment: catalytic domain. Unp residues 76-1108. Synonym: alpha-mannosidase ii, mannosyl-oligosaccharide 1, 3-1,6-alpha-mannosidase, man ii, golgi alpha-mannosidase ii, aman ii. Engineered: yes. Mutation: yes
Source: Drosophila melanogaster. Fruit fly. Gene: alpha-man-ii, gmii. Expressed in: drosophila melanogaster.
Resolution:
1.10Å     R-factor:   0.158     R-free:   0.190
Authors: D.A.Kuntz,D.R.Rose
Date:
07-Jan-08     Release date:   01-Jul-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.
1016 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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