Research workbench
Crystal structure of giardia lamblia HOP2-MND1 complex
Analyse Crystal structure of giardia lamblia HOP2-MND1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y66
- Type
- protein
- Length
- 1,002 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MND1; Putative tbpip family protein
- UniProt
- E2RTU1, V6TR15
- Pockets
- 5 · best druggability 0.54
Structure
x-ray diffraction · 6 distinct chains · 72% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MND1 | protein | 128 | 80% helix, 0% strand | E2RTU1 |
| B | Putative tbpip family protein | protein | 152 | 77% helix, 0% strand | V6TR15 |
| C | MND1 | protein | 197 | 71% helix, 5% strand | E2RTU1 |
| D | Putative tbpip family protein | protein | 208 | 68% helix, 3% strand | V6TR15 |
| E | MND1 | protein | 150 | 71% helix, 5% strand | E2RTU1 |
| F | Putative tbpip family protein | protein | 167 | 69% helix, 8% strand | V6TR15 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.54 | 0.87 | 19 | empty |
| 2 | 75 | 0.46 | 0.82 | 20 | empty |
| 3 | 111 | 0.40 | 0.76 | 26 | empty |
| 4 | 116 | 0.36 | 0.73 | 21 | empty |
| 5 | 54 | 0.30 | 0.76 | 14 | empty |
Interfaces
11 interfaces between chains.
- C–D · 3870 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 2849 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 2390 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 393 Ų buried · 5 hydrogen bonds · protein-protein
- D–F · 282 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4Y66 · Crystal structure of Giardia lamblia Hop2-Mnd1 complex · 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 E2RTU1
- Every structure of UniProt V6TR15
- Elsewhere: RCSB PDB 4Y66 · PDBe 4Y66 · UniProt E2RTU1 · UniProt V6TR15
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