MolNFT v1 · #149861 · protein
Truncated ftsh from a. aeolicus in R32
6GCN · ATP-dependent zinc metalloprotease ftsh: “Truncated ftsh from a. aeolicus in R32”. X-ray diffraction, 2 ligands (ADP, ZN), 20 pockets (best druggability 0.77). MolNFT v1 #149861 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6GCN
- Type
- protein
- Length
- 1,719 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent zinc metalloprotease ftsh
- EC
- 3.4.24.-
- UniProt
- O67077
- Ligands
- ADP, ZN
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 57% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 418 | 57% helix, 10% strand | O67077 |
| B | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 440 | 57% helix, 7% strand | O67077 |
| C | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 424 | 56% helix, 9% strand | O67077 |
| D | ATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-) | protein | 437 | 57% helix, 8% strand | O67077 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1010 | 0.77 | 0.79 | 97 | empty |
| 2 | 534 | 0.63 | 0.75 | 62 | ADP |
| 3 | 417 | 0.63 | 0.77 | 38 | empty |
| 4 | 376 | 0.61 | 0.77 | 42 | empty |
| 5 | 383 | 0.61 | 0.77 | 49 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1982 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 1908 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 441 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 417 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 292 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 O67077
- Elsewhere: RCSB PDB 6GCN · PDBe 6GCN · UniProt O67077
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