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Crystal structure of hmp-1 M domain
Analyse Crystal structure of hmp-1 M domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H5M
- Type
- protein
- Length
- 707 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-catenin-like protein hmp-1
- UniProt
- P90947
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-catenin-like protein hmp-1 | protein | 358 | 85% helix, 0% strand | P90947 |
| B | Alpha-catenin-like protein hmp-1 | protein | 349 | 85% helix, 0% strand | P90947 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.76 | 0.79 | 89 | empty |
| 2 | 193 | 0.45 | 0.74 | 21 | empty |
| 3 | 50 | 0.36 | 0.80 | 12 | empty |
| 4 | 51 | 0.34 | 0.79 | 17 | empty |
| 5 | 76 | 0.33 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 945 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 P90947
- Elsewhere: RCSB PDB 5H5M · PDBe 5H5M · UniProt P90947
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