PDB ID:  pdb_00007ni1
  • CRYSTAL STRUCTURE OF NATIVE HUMAN MYELOPEROXIDASE IN COMPLEX WITH CPD 9
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.11 Å
  • Deposition date: 2021-02-11
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 E (NAGStructure of NAGNAG , BMAStructure of BMABMA , MANStructure of MANMAN , FUCStructure of FUCFUC ), G (CLStructure of CLCL ), H (CLStructure of CLCL ), M (CAStructure of CACA ), N (CLStructure of CLCL ), O (CLStructure of CLCL ), P (NAGStructure of NAGNAG ), Q (NAGStructure of NAGNAG ), R (UEBStructure of UEBUEB ), S (BMAStructure of BMABMA )
Each chain information

Showing 1 chain with heme of 2. Show all chains

Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 114-577 (279-744)
Missing residues 150CYS-150CYS
Nonstandard amino acids Structure of CSOCSO
Uniprot ID P05164 →UniprotKB
S-S bonds 115:125,119:143,221:232,440:497,538:564
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_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 (NAGStructure of NAGNAG , BMAStructure of BMABMA , MANStructure of MANMAN , FUCStructure of FUCFUC ), J (CLStructure of CLCL ), K (CLStructure of CLCL ), T (BMAStructure of BMABMA ), U (CLStructure of CLCL ), V (NAGStructure of NAGNAG ), W (NAGStructure of NAGNAG ), X (CAStructure of CACA ), Y (UEBStructure of UEBUEB )
Each chain information

Showing 1 chain with heme of 2. Show all chains

Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 114-577 (279-744)
Missing residues 150CYS-150CYS
Nonstandard amino acids Structure of CSOCSO
Uniprot ID P05164 →UniprotKB
S-S bonds 115:125,119:143,221:232,440:497,538:564
label_asym_ids of heme L
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.09 Å