MolNFT v1 · #12735 · protein
Crystal structure of a THY1-complementing protein (TM0449) from thermotoga maritima at 2.25 a resolution
1KQ4 · Hypothetical protein TM0449: “Crystal structure of a THY1-complementing protein (TM0449) from thermotoga maritima at 2.25 a resolution”. X-ray diffraction, 1 ligand (FAD), 7 pockets (best druggability 0.85). MolNFT v1 #12735 on…
- PDB
- 1KQ4
- Type
- protein
- Length
- 838 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TM0449
- UniProt
- Q9WYT0
- Ligands
- FAD
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 52% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein TM0449 | protein | 203 | 53% helix, 19% strand | Q9WYT0 |
| B | Hypothetical protein TM0449 | protein | 211 | 52% helix, 18% strand | Q9WYT0 |
| C | Hypothetical protein TM0449 | protein | 214 | 52% helix, 18% strand | Q9WYT0 |
| D | Hypothetical protein TM0449 | protein | 210 | 51% helix, 18% strand | Q9WYT0 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, C, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.85 | 0.90 | 56 | FAD |
| 2 | 259 | 0.72 | 0.86 | 36 | FAD |
| 3 | 142 | 0.70 | 0.90 | 26 | empty |
| 4 | 76 | 0.62 | 0.90 | 18 | empty |
| 5 | 127 | 0.61 | 0.85 | 22 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2191 Ų buried · 28 hydrogen bonds · protein-protein
- A–D · 2114 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 1328 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1167 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 233 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 1KQ4 · Crystal structure of a THY1-complementing protein (TM0449) from thermotoga maritima at… · 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 Q9WYT0
- Elsewhere: RCSB PDB 1KQ4 · PDBe 1KQ4 · UniProt Q9WYT0
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