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Crystal Structure of Uroporphyrinogen Decarboxylase from Bacillus subtilis
Analyse Crystal Structure of Uroporphyrinogen Decarboxylase from Bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2INF
- Type
- protein
- Length
- 1,376 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Bacillus subtilis
- Molecule
- Uroporphyrinogen decarboxylase
- EC
- 4.1.1.37
- UniProt
- P32395
- Pockets
- 18 · best druggability 0.85
Structure
x-ray diffraction · resolution 2.3 · 1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Uroporphyrinogen decarboxylase (EC 4.1.1.37) | protein | 344 | 53% helix, 10% strand | P32395 |
Pockets
18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.85 | 0.86 | 124 | empty |
| 2 | 641 | 0.81 | 0.86 | 79 | empty |
| 3 | 483 | 0.78 | 0.85 | 47 | empty |
| 4 | 317 | 0.74 | 0.86 | 33 | empty |
| 5 | 285 | 0.73 | 0.86 | 38 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1261 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1251 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 428 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 400 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2INF · Crystal structure of uroporphyrinogen decarboxylase from bacillus subtilis · the same entry in another collection · chain D against D, TM-score 1.00
- P32395 · AlphaFold monomer V2.0 prediction for uroporphyrinogen decarboxylase (P32395) · a predicted model of the same protein · chain B 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 P32395
- Elsewhere: RCSB PDB 2INF · PDBe 2INF · UniProt P32395
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