MolNFT v1 · #104193 · protein
Crystal structure of the hypothetical protein TM0182 thermotoga maritima, N-terminal domain.
4Q37 · Radical SAM protein: “Crystal structure of the hypothetical protein TM0182 thermotoga maritima, N-terminal domain.”. X-ray diffraction, 1 ligand (PT), 11 pockets (best druggability 0.71). MolNFT v1 #104193 on GenesisL1: 3D…
- PDB
- 4Q37
- Type
- protein
- Length
- 704 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Radical SAM protein
- UniProt
- Q9WY26
- Ligands
- PT
- Pockets
- 11 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F | Radical SAM protein | protein | 120 | 36% helix, 21% strand | Q9WY26 |
| E | Radical SAM protein | protein | 104 | 37% helix, 17% strand | Q9WY26 |
Ligands and binding sites
- PT · Platinum (II) ion · metal · 2 copies · chains A, E, D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 492 | 0.71 | 0.80 | 67 | PT |
| 2 | 355 | 0.66 | 0.80 | 33 | empty |
| 3 | 439 | 0.66 | 0.78 | 41 | empty |
| 4 | 277 | 0.65 | 0.82 | 30 | PT |
| 5 | 149 | 0.48 | 0.77 | 27 | empty |
Interfaces
7 interfaces between chains.
- A–E · 1987 Ų buried · 37 hydrogen bonds · protein-protein
- D–F · 1909 Ų buried · 29 hydrogen bonds · protein-protein
- C–D · 414 Ų buried · 6 hydrogen bonds · protein-protein
- A–F · 413 Ų buried · 5 hydrogen bonds · protein-protein
- D–E · 373 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4Q37 · Crystal structure of the hypothetical protein TM0182 Thermotoga maritima, N-terminal… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9WY26
- Elsewhere: RCSB PDB 4Q37 · PDBe 4Q37 · UniProt Q9WY26
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