Research workbench
The crystal structure of catalase-peroxidase, katg, from synechococcus PCC7942
Analyse The crystal structure of catalase-peroxidase, katg, from synechococcus PCC7942 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WNU
- Type
- protein
- Length
- 710 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catalase-peroxidase
- EC
- 1.11.1.21
- UniProt
- Q31MN3
- Ligands
- HEB, NA
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catalase-peroxidase (EC 1.11.1.21) | protein | 710 | 45% helix, 7% strand | Q31MN3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 554 | 0.82 | 0.87 | 69 | HEB |
| 2 | 625 | 0.71 | 0.79 | 59 | empty |
| 3 | 469 | 0.64 | 0.77 | 46 | empty |
| 4 | 101 | 0.60 | 0.87 | 38 | empty |
| 5 | 62 | 0.35 | 0.77 | 11 | empty |
Compared structures
- 3WNU · The crystal structure of catalase-peroxidase, KatG, from Synechococcus PCC7942 · the same entry in another collection · chain A against A, TM-score 1.00
- Q31MN3 · AlphaFold monomer V2.0 prediction for catalase-peroxidase (Q31MN3) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q31MN3
- Elsewhere: RCSB PDB 3WNU · PDBe 3WNU · UniProt Q31MN3
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