Danish
PDB ID:  pdb_00002xq1
  • Crystal structure of peroxisomal catalase from the yeast Hansenula polymorpha
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.9 Å
  • Deposition date: 2010-08-31
Number of assemblies:  4
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 4
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others
Each chain information
Chain M heme  
auth_asym_id M
Residue indices (Uniprot) 4-500 (1-507)
Mutations (UniProt numbering)
Missing residues 409PRO-415LYS
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme BA
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 1.16 Å
Chain N heme  
auth_asym_id N
Residue indices (Uniprot) 2-500 (1-507)
Mutations (UniProt numbering)
Missing residues 409PRO-416PRO
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme CA
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Chain O heme  
auth_asym_id O
Residue indices (Uniprot) 4-500 (1-507)
Mutations (UniProt numbering)
Missing residues 409PRO-413GLY
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme DA
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain P heme  
auth_asym_id P
Residue indices (Uniprot) 4-500 (1-507)
Mutations (UniProt numbering)
Missing residues 408SER-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme EA
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.09 Å
Assembly ID:  2  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 4
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others
Each chain information

Showing all 4 chains (3 with heme). Show only chains with heme

Chain A  
auth_asym_id A
Residue indices (Uniprot) 4-500 (1-507)
Mutations (UniProt numbering)
Missing residues 409PRO-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 2-500 (1-507)
Mutations (UniProt numbering)
Missing residues 408SER-413GLY
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme Q
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 4-500 (1-507)
Mutations (UniProt numbering)
Missing residues 408SER-413GLY
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme R
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 2-500 (1-507)
Mutations (UniProt numbering)
Missing residues 408SER-413GLY
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme S
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Assembly ID:  3  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 4
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others
Each chain information
Chain I heme  
auth_asym_id I
Residue indices (Uniprot) 4-500 (1-507)
Mutations (UniProt numbering)
Missing residues 409PRO-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme X
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain J heme  
auth_asym_id J
Residue indices (Uniprot) 2-500 (1-507)
Mutations (UniProt numbering)
Missing residues 407VAL-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme Y
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain K heme  
auth_asym_id K
Residue indices (Uniprot) 4-500 (1-507)
Mutations (UniProt numbering)
Missing residues 407VAL-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme Z
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
Chain L heme  
auth_asym_id L
Residue indices (Uniprot) 6-500 (1-507)
Mutations (UniProt numbering)
Missing residues 408SER-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme AA
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
Assembly ID:  4  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 4
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others
Each chain information
Chain E heme  
auth_asym_id E
Residue indices (Uniprot) 5-500 (1-507)
Mutations (UniProt numbering)
Missing residues 408SER-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme T
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
Chain F heme  
auth_asym_id F
Residue indices (Uniprot) 2-500 (1-507)
Mutations (UniProt numbering)
Missing residues 408SER-413GLY
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme U
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain G heme  
auth_asym_id G
Residue indices (Uniprot) 4-500 (1-507)
Mutations (UniProt numbering)
Missing residues 408SER-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme V
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
Chain H heme  
auth_asym_id H
Residue indices (Uniprot) 6-500 (1-507)
Mutations (UniProt numbering)
Missing residues 406ALA-414ASN
Structural gaps Exists
Uniprot ID P30263 ￫UniprotKB
label_asym_ids of heme W
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.15 Å