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PDBsum entry 2c9h

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protein metals links
Transferase PDB id
2c9h
Jmol
Contents
Protein chain
427 a.a. *
Metals
_NI
Waters ×235
* Residue conservation analysis
PDB id:
2c9h
Name: Transferase
Title: Structure of mitochondrial beta-ketoacyl synthase
Structure: Mitochondrial beta-ketoacyl synthase. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_cell_line: de3-r3.
Biol. unit: Dimer (from PDB file)
Resolution:
1.80Å     R-factor:   0.181     R-free:   0.240
Authors: G.Bunkoczi,X.Wu,C.Smee,O.Gileadi,C.Arrowsmith,A.Edwards,M.Su J.Weigelt,F.Von Delft,U.Oppermann
Key ref: G.Bunkoczi et al. Structure of mitochondrial beta-Ketoacyl synthase. To be published, .
Date:
12-Dec-05     Release date:   13-Dec-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9NWU1  (OXSM_HUMAN) -  3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
Seq:
Struc:
459 a.a.
427 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.41  - Beta-ketoacyl-[acyl-carrier-protein] synthase I.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO2 + [acyl-carrier-protein]
Acyl-[acyl-carrier-protein]
+ malonyl-[acyl-carrier-protein]
= 3-oxoacyl- [acyl-carrier-protein]
+ CO(2)
+ [acyl-carrier-protein]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrion   1 term 
  Biological process     metabolic process   7 terms 
  Biochemical function     catalytic activity     5 terms