Research workbench
Crystal structure of fungal MAGKATG2
Analyse Crystal structure of fungal MAGKATG2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UT2
- Type
- protein
- Length
- 1,467 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catalase-peroxidase 2
- EC
- 1.11.1.21
- UniProt
- A4QUT2
- Ligands
- HEM
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catalase-peroxidase 2 (EC 1.11.1.21) | protein | 735 | 44% helix, 8% strand | A4QUT2 |
| B | Catalase-peroxidase 2 (EC 1.11.1.21) | protein | 732 | 44% helix, 7% strand | A4QUT2 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 885 | 0.88 | 0.91 | 96 | empty |
| 2 | 552 | 0.80 | 0.86 | 74 | HEM |
| 3 | 510 | 0.80 | 0.86 | 73 | HEM |
| 4 | 78 | 0.74 | 0.98 | 19 | empty |
| 5 | 75 | 0.74 | 0.98 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 5052 Ų buried · 79 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
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 A4QUT2
- Elsewhere: RCSB PDB 3UT2 · PDBe 3UT2 · UniProt A4QUT2
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