MolNFT v1 · #104095 · protein
Crystal structure of thermotoga maritima ftsh periplasmic domain
4Q0F · ATP-dependent zinc metalloprotease ftsh: “Crystal structure of thermotoga maritima ftsh periplasmic domain”. X-ray diffraction, 1 pocket (best druggability 0.46). MolNFT v1 #104095 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4Q0F
- Type
- protein
- Length
- 202 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent zinc metalloprotease ftsh
- EC
- 3.4.24.-
- UniProt
- Q9WZ49
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 68 | 31% helix, 35% strand | Q9WZ49 |
| B | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 67 | 31% helix, 33% strand | Q9WZ49 |
| C | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 67 | 33% helix, 34% strand | Q9WZ49 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.46 | 0.80 | 18 | empty |
Interfaces
2 interfaces between chains.
- A–C · 549 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 533 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4Q0F · Crystal Structure of Thermotoga maritima FtsH Periplasmic domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WZ49 · AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (Q9WZ49) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9WZ49
- Elsewhere: RCSB PDB 4Q0F · PDBe 4Q0F · UniProt Q9WZ49
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