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Crystal structure of the C-terminal domain from the catalase-peroxidase katg of escherichia COLI (P21 21 21)
Analyse Crystal structure of the C-terminal domain from the catalase-peroxidase katg of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U2J
- Type
- protein
- Length
- 2,360 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PEROXIDASE/CATALASE hpi
- EC
- 1.11.1.6
- UniProt
- P13029
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | PEROXIDASE/CATALASE hpi (EC 1.11.1.6) | protein | 295 | 47% helix, 8% strand | P13029 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 757 | 0.80 | 0.84 | 69 | empty |
| 2 | 638 | 0.80 | 0.85 | 68 | empty |
| 3 | 720 | 0.77 | 0.82 | 83 | empty |
| 4 | 732 | 0.77 | 0.81 | 52 | empty |
| 5 | 595 | 0.74 | 0.81 | 73 | empty |
Interfaces
13 interfaces between chains.
- A–C · 775 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 751 Ų buried · 5 hydrogen bonds · protein-protein
- E–G · 543 Ų buried · 11 hydrogen bonds · protein-protein
- G–H · 499 Ų buried · 5 hydrogen bonds · protein-protein
- E–F · 487 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1U2J · Crystal structure of the C-terminal domain from the catalase-peroxidase KatG of… · the same entry in another collection · chain H against H, TM-score 1.00
- P13029 · AlphaFold monomer V2.0 prediction for catalase-peroxidase (P13029) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P13029
- Elsewhere: RCSB PDB 1U2J · PDBe 1U2J · UniProt P13029
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