PDB ID: pdb_00003f9p
- Crystal structure of myeloperoxidase from human leukocytes
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.93 Å
- Deposition date: 2008-11-14
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
, FUC FUC
), G (CL CL
), I (CA CA
), J (NAGNAG
), K (NAGNAG
), L (ACT ACT
)
|
Each chain information
Showing all 2 chains (1 with heme). Show only chains with heme
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 0-106 (165-278) |
| 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) | 113-578 (279-745) |
| Missing residues | 150CYS-150CYS |
| Structural gaps | Exists |
| Nonstandard amino acids |
 CSO
|
| Uniprot ID | P05164 ￫UniprotKB |
| S-S bonds | 115:125,119:143,221:232,440:497,538:564 |
| 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
, FUCFUC
), N (CACA
), O (CLCL
), P (NAGNAG
), Q (NAGNAG
), R (ACTACT
)
|
Each chain information
Showing all 2 chains (1 with heme). Show only chains with heme
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 0-106 (165-278) |
| 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) | 113-578 (279-745) |
| Missing residues | 150CYS-150CYS |
| Structural gaps | Exists |
| Nonstandard amino acids |
CSO
|
| Uniprot ID | P05164 ￫UniprotKB |
| S-S bonds | 115:125,119:143,221:232,440:497,538:564 |
| label_asym_ids of heme | M |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.08 Å |