Research workbench
Crystal structure of thermotoga maritima ftsh periplasmic domain
Analyse Crystal structure of thermotoga maritima ftsh periplasmic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M8A
- Type
- protein
- Length
- 203 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 · 2 distinct chains · 33% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 67 | 31% helix, 33% strand | Q9WZ49 |
| B, C | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 68 | 34% helix, 35% strand | Q9WZ49 |
Ligands and binding sites
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 87 | 0.46 | 0.81 | 19 | empty |
Interfaces
2 interfaces between chains.
- B–C · 555 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 550 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4M8A · 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 B 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 4M8A · PDBe 4M8A · UniProt Q9WZ49
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