PDB ID: pdb_00006pt7
- Structure of KatE1 catalase from Acinetobacter sp. Ver3
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.15 Å
- Deposition date: 2019-07-15
Number of assemblies: 1
| Structural data | modeled |
|---|---|
| Oligomeric count | 4 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
B (NAP  NAP
), B-1 (NAPNAP
), B-2 (NAPNAP
), B-3 (NAPNAP
), D (CL CL
), D-1 (CLCL
), D-2 (CLCL
), D-3 (CLCL
), E (UNX UNX
), E-1 (UNXUNX
), E-2 (UNXUNX
), E-3 (UNXUNX
), F (UNXUNX
), F-1 (UNXUNX
), F-2 (UNXUNX
), F-3 (UNXUNX
), G (UNXUNX
), G-1 (UNXUNX
), G-2 (UNXUNX
), G-3 (UNXUNX
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 7-506 (7-506) |
| Mutations (UniProt numbering) | |
| Missing residues | 60MET-60MET |
| Nonstandard amino acids |
 OMT
|
| Uniprot ID | A0A1A7RA38 ￫UniprotKB |
| label_asym_ids of heme | C |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 7-506 (7-506) |
| Mutations (UniProt numbering) | |
| Missing residues | 60MET-60MET |
| Nonstandard amino acids |
OMT
|
| Uniprot ID | A0A1A7RA38 ￫UniprotKB |
| label_asym_ids of heme | C-1 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.08 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 7-506 (7-506) |
| Mutations (UniProt numbering) | |
| Missing residues | 60MET-60MET |
| Nonstandard amino acids |
OMT
|
| Uniprot ID | A0A1A7RA38 ￫UniprotKB |
| label_asym_ids of heme | C-2 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.08 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 7-506 (7-506) |
| Mutations (UniProt numbering) | |
| Missing residues | 60MET-60MET |
| Nonstandard amino acids |
OMT
|
| Uniprot ID | A0A1A7RA38 ￫UniprotKB |
| label_asym_ids of heme | C-3 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.08 Å |