PDB ID:  pdb_00004gt2
  • Crystal structure of DyP-type peroxidase (SCO3963) from Streptomyces coelicolor
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 1.8 Å
  • Deposition date: 2012-08-28
Number of assemblies:  2
Assembly ID:  1  (author_and_software_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 (GOLStructure of GOLGOL ), G (OXYStructure of OXYOXY ), H (ACTStructure of ACTACT ), I (GOLStructure of GOLGOL ), K (GOLStructure of GOLGOL ), L (OXYStructure of OXYOXY ), M (GOLStructure of GOLGOL )
Each chain information
Chain A heme  
auth_asym_id B
Residue indices (Uniprot) 69-445 (1-445)
Missing residues 272GLU-279GLY
Structural gaps Exists
Uniprot ID Q9ZBW9 →UniprotKB
label_asym_ids of heme E
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
Chain B heme  
auth_asym_id A
Residue indices (Uniprot) 69-445 (1-445)
Missing residues 273PRO-278GLY
Structural gaps Exists
Uniprot ID Q9ZBW9 →UniprotKB
label_asym_ids of heme J
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
Assembly ID:  2  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others O (GOLStructure of GOLGOL ), P (GOLStructure of GOLGOL ), Q (OXYStructure of OXYOXY ), R (GOLStructure of GOLGOL ), T (OXYStructure of OXYOXY ), U (GOLStructure of GOLGOL )
Each chain information
Chain C heme  
auth_asym_id E
Residue indices (Uniprot) 69-445 (1-445)
Missing residues 273PRO-279GLY
Structural gaps Exists
Uniprot ID Q9ZBW9 →UniprotKB
label_asym_ids of heme N
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
Chain D heme  
auth_asym_id G
Residue indices (Uniprot) 69-445 (1-445)
Missing residues 272GLU-279GLY
Structural gaps Exists
Uniprot ID Q9ZBW9 →UniprotKB
label_asym_ids of heme S
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å