Research workbench
Structure of proteus mirabilis pr catalase for the native form (E- FE(III)) complexed with NADPH
Analyse Structure of proteus mirabilis pr catalase for the native form (E- FE(III))… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CAH
- Type
- protein
- Length
- 475 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catalase
- EC
- 1.11.1.6
- UniProt
- P42321
- Ligands
- HEM, NDP
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catalase (EC 1.11.1.6) | protein | 475 | 33% helix, 17% strand | P42321 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.77 | 0.87 | 43 | HEM |
| 2 | 267 | 0.64 | 0.81 | 43 | NDP |
| 3 | 216 | 0.54 | 0.78 | 26 | empty |
| 4 | 318 | 0.54 | 0.75 | 32 | empty |
| 5 | 209 | 0.48 | 0.75 | 25 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 2CAH · Structure of proteus mirabilis pr catalase for the native form (E-FE(III)) complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P42321 · AlphaFold monomer V2.0 prediction for catalase (P42321) · 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 P42321
- Elsewhere: RCSB PDB 2CAH · PDBe 2CAH · UniProt P42321
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