Research workbench
Crystal structure of hslv from thermotoga maritima
Analyse Crystal structure of hslv from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M4Y
- Type
- protein
- Length
- 513 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease hslv
- EC
- 3.4.25.-
- UniProt
- Q9WYZ1
- Ligands
- NA
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | ATP-dependent protease hslv (EC 3.4.25.-) | protein | 171 | 37% helix, 28% strand | Q9WYZ1 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.63 | 0.77 | 69 | empty |
| 2 | 290 | 0.57 | 0.77 | 34 | empty |
Interfaces
2 interfaces between chains.
- A–B · 794 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 775 Ų buried · 13 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 Q9WYZ1
- Elsewhere: RCSB PDB 1M4Y · PDBe 1M4Y · UniProt Q9WYZ1
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