Research workbench
Crystal structures of trypanosoma bruciei MRP1/MRP2
Analyse Crystal structures of trypanosoma bruciei MRP1/MRP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GIA
- Type
- protein
- Length
- 601 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial RNA-binding protein 2; Mitochondrial RNA-binding protein 1
- UniProt
- Q952G2, P90629
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial RNA-binding protein 2 | protein | 154 | 31% helix, 40% strand | Q952G2 |
| B, D | Mitochondrial RNA-binding protein 1 | protein | 146 | 26% helix, 38% strand | P90629 |
| G | Mitochondrial RNA-binding protein 2 | protein | 155 | 27% helix, 39% strand | Q952G2 |
Ligands and binding sites
- ACY · Acetic acid · additive · 2 copies · chains A, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 763 | 0.74 | 0.79 | 72 | empty |
| 2 | 293 | 0.60 | 0.79 | 41 | empty |
| 3 | 270 | 0.60 | 0.79 | 29 | empty |
| 4 | 145 | 0.51 | 0.79 | 23 | empty |
| 5 | 67 | 0.27 | 0.73 | 19 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1248 Ų buried · 8 hydrogen bonds · protein-protein
- B–G · 1182 Ų buried · 10 hydrogen bonds · protein-protein
- D–G · 753 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 749 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 58 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2GIA · Crystal structures of trypanosoma bruciei MRP1/MRP2 · 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 Q952G2
- Every structure of UniProt P90629
- Elsewhere: RCSB PDB 2GIA · PDBe 2GIA · UniProt Q952G2 · UniProt P90629
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