PDB ID: pdb_00003zs1
- Human Myeloperoxidase inactivated by TX5
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.6 Å
- Deposition date: 2011-06-21
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 |
AA (NAG  NAG
), F (NAGNAG
, BMA BMA
), J (PVW PVW
), T (SO4 SO4
), U (CA CA
), V (CL CL
), W (ACT ACT
), X (ACTACT
), Y (ACTACT
), Z (NAGNAG
)
|
Each chain information
Showing all 2 chains (1 with heme). Show only chains with heme
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 1-104 (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 |
| 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 | I |
| 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 |
E (NAGNAG
, BMABMA
, FUC FUC
), H (PVWPVW
), K (SO4SO4
), L (CACA
), M (CLCL
), N (SO4SO4
), O (ACTACT
), P (ACTACT
), Q (ACTACT
), R (NAGNAG
), S (NAGNAG
)
|
Each chain information
Showing all 2 chains (1 with heme). Show only chains with heme
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-104 (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 |
| 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 | G |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |