Research workbench
The structure of mfpa (RV3361C, P21 crystal form). the pentapeptide repeat protein from mycobacterium tuberculosis folds as a right-handed quadrilateral beta- helix.
Analyse The structure of mfpa (RV3361C, P21 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
- 2BM5
- Type
- protein
- Length
- 363 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pentapeptide repeat family protein
- UniProt
- O50390
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pentapeptide repeat family protein | protein | 183 | 9% helix, 32% strand | O50390 |
| B | Pentapeptide repeat family protein | protein | 180 | 9% helix, 33% strand | O50390 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 823 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2BM5 · The Structure of MfpA (Rv3361c, P21 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 2BM5 · PDBe 2BM5 · UniProt O50390
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