Research workbench
The structure of mfpa (RV3361C, P3221 crystal form). the pentapeptide repeat protein from mycobacterium tuberculosis folds as a right-handed quadrilateral beta- helix.
Analyse The structure of mfpa (RV3361C, P3221 crystal form). the pentapeptide repeat… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BM7
- Type
- protein
- Length
- 539 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pentapeptide repeat family protein
- UniProt
- O50390
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pentapeptide repeat family protein | protein | 178 | 7% helix, 31% strand | O50390 |
| B | Pentapeptide repeat family protein | protein | 181 | 7% helix, 31% strand | O50390 |
| C | Pentapeptide repeat family protein | protein | 180 | 8% helix, 32% strand | O50390 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.79 | 0.86 | 63 | empty |
| 2 | 159 | 0.64 | 0.86 | 26 | empty |
| 3 | 60 | 0.46 | 0.84 | 18 | empty |
| 4 | 153 | 0.45 | 0.76 | 25 | empty |
Interfaces
3 interfaces between chains.
- B–C · 725 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 386 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 258 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2BM7 · The Structure of MfpA (Rv3361c, P3221 Crystal form). The Pentapeptide Repeat Protein from… · the same entry in another collection · 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 O50390
- Elsewhere: RCSB PDB 2BM7 · PDBe 2BM7 · UniProt O50390
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