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PDBsum entry 3n83

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3n83
Jmol
Contents
Protein chain
(+ 2 more) 494 a.a.
Ligands
GAI ×16
EDO ×23
ADP ×8
Metals
_NA ×8
Waters ×2933
PDB id:
3n83
Name: Oxidoreductase
Title: T244a mutant of human mitochondrial aldehyde dehydrogenase, complex
Structure: Aldehyde dehydrogenase, mitochondrial. Chain: a, b, c, d, e, f, g, h. Fragment: mature sequence, residues 18-517. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: aldh2, aldm. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.90Å     R-factor:   0.191     R-free:   0.232
Authors: L.Gonzalez-Segura,T.D.Hurley
Key ref: K.-K.Ho et al. Conformational selection during catalysis: the role o threonine 244 in aldh2. To be published, .
Date:
27-May-10     Release date:   13-Apr-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P05091  (ALDH2_HUMAN) -  Aldehyde dehydrogenase, mitochondrial
Seq:
Struc:
517 a.a.
494 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.1.2.1.3  - Aldehyde dehydrogenase (NAD(+)).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An aldehyde + NAD+ + H2O = a carboxylate + NADH
aldehyde
Bound ligand (Het Group name = EDO)
matches with 40.00% similarity
+
NAD(+)
Bound ligand (Het Group name = ADP)
matches with 61.36% similarity
+ H(2)O
= carboxylate
+ NADH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular vesicular exosome   3 terms 
  Biological process     metabolic process   10 terms 
  Biochemical function     electron carrier activity     5 terms