PDB ID: pdb_00005fiw
- CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE AT 1.7 ANGSTROMS RESOLUTION
- Experimental method: X-RAY DIFFRACTION
- Resolution: 1.7 Å
- Deposition date: 2015-10-02
Number of assemblies: 2
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
E (NAG  NAG
, BMA BMA
), G (CL CL
), K (CA CA
), L (CLCL
), M (CLCL
), N (NAGNAG
), O (NAGNAG
), P (BMABMA
), V (MAN MAN
), W (FUC FUC
)
|
Each chain information
Showing all 2 chains (1 with heme). Show only chains with heme
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-105 (167-271) |
| Uniprot ID | P05164 ￫UniprotKB |
| S-S bonds | 1:14 |
| label_asym_ids of heme | None |
| Available structure | PDB |
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 114-577 (279-744) |
| Missing residues | 150CYS-150CYS |
| Nonstandard amino acids |
 CSO
|
| Uniprot ID | P05164 ￫UniprotKB |
| S-S bonds | 115:125,119:143,221:232,538:564 |
| label_asym_ids of heme | H |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.10 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
F (NAGNAG
, BMABMA
), I (CLCL
), Q (CLCL
), R (NAGNAG
), S (NAGNAG
), T (BMABMA
), U (CACA
), X (MANMAN
), Y (FUCFUC
)
|
Each chain information
Showing all 2 chains (1 with heme). Show only chains with heme
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 1-103 (167-271) |
| Uniprot ID | P05164 ￫UniprotKB |
| S-S bonds | 1:14 |
| label_asym_ids of heme | None |
| Available structure | PDB |
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 114-577 (279-744) |
| Missing residues | 150CYS-150CYS |
| Nonstandard amino acids |
CSO
|
| Uniprot ID | P05164 ￫UniprotKB |
| S-S bonds | 115:125,119:143,221:232,538:564 |
| label_asym_ids of heme | J |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.08 Å |