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PDBsum entry 3e04

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protein ligands Protein-protein interface(s) links
Lyase PDB id
3e04
Jmol
Contents
Protein chains
456 a.a. *
415 a.a. *
Ligands
EDO ×3
Waters ×655
* Residue conservation analysis
PDB id:
3e04
Name: Lyase
Title: Crystal structure of human fumarate hydratase
Structure: Fumarate hydratase. Chain: a, b, c, d. Fragment: unp residues 44-510. Synonym: fumarase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fh. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.95Å     R-factor:   0.197     R-free:   0.244
Authors: K.L.Kavanagh,U.Oppermann,Structural Genomics Consortium (Sgc
Key ref: K.L.Kavanagh et al. Crystal structure of human fumarate hydratase. To be published, .
Date:
30-Jul-08     Release date:   12-Aug-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P07954  (FUMH_HUMAN) -  Fumarate hydratase, mitochondrial
Seq:
Struc:
510 a.a.
456 a.a.
Protein chain
Pfam   ArchSchema ?
P07954  (FUMH_HUMAN) -  Fumarate hydratase, mitochondrial
Seq:
Struc:
510 a.a.
415 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 9 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.4.2.1.2  - Fumarate hydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Citric acid cycle
      Reaction: (S)-malate = fumarate + H2O
(S)-malate
Bound ligand (Het Group name = EDO)
matches with 44.44% similarity
= fumarate
+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   5 terms 
  Biological process     small molecule metabolic process   5 terms 
  Biochemical function     catalytic activity     3 terms