PDB ID:  pdb_00005k91
  • Crystal structure of dimeric chlorite dismutase from Cyanothece sp. PCC7425 in complex with fluoride
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 1.18 Å
  • Deposition date: 2016-05-31
Number of assemblies:  2
Assembly ID:  1  (author_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others F (FStructure of FF ), G (GOLStructure of GOLGOL ), H (SO4Structure of SO4SO4 ), J (FStructure of FF ), K (GOLStructure of GOLGOL )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 2-182 (2-182)
Mutations (UniProt numbering)
Missing residues 41VAL-47ASP
Structural gaps Exists
Uniprot ID B8HNS6 →UniprotKB
label_asym_ids of heme E
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 2-182 (2-182)
Mutations (UniProt numbering)
Missing residues 41VAL-46LEU
Structural gaps Exists
Uniprot ID B8HNS6 →UniprotKB
label_asym_ids of heme I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.09 Å
Assembly ID:  2  (author_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others M (FStructure of FF ), N (GOLStructure of GOLGOL ), P (FStructure of FF ), Q (GOLStructure of GOLGOL ), R (SO4Structure of SO4SO4 )
Each chain information
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 2-182 (2-182)
Mutations (UniProt numbering)
Missing residues 41VAL-46LEU
Structural gaps Exists
Uniprot ID B8HNS6 →UniprotKB
label_asym_ids of heme L
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 2-182 (2-182)
Mutations (UniProt numbering)
Missing residues 41VAL-46LEU
Structural gaps Exists
Uniprot ID B8HNS6 →UniprotKB
label_asym_ids of heme O
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å