MolNFT v1 · #106681 · protein
Crystal structure of eutl from clostridium perfringens at 298K
4TM6 · Ethanolamine utilization protein eutl: “Crystal structure of eutl from clostridium perfringens at 298K”. X-ray diffraction, 1 ligand (NA), 7 pockets (best druggability 0.50). MolNFT v1 #106681 on GenesisL1: 3D structure, binding…
- PDB
- 4TM6
- Type
- protein
- Length
- 661 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ethanolamine utilization protein eutl
- UniProt
- B1BQ33
- Ligands
- NA
- Pockets
- 7 · best druggability 0.50
Structure
x-ray diffraction · 3 distinct chains · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ethanolamine utilization protein eutl | protein | 217 | 37% helix, 27% strand | B1BQ33 |
| B | Ethanolamine utilization protein eutl | protein | 219 | 36% helix, 26% strand | B1BQ33 |
| C | Ethanolamine utilization protein eutl | protein | 225 | 38% helix, 26% strand | B1BQ33 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.50 | 0.79 | 21 | empty |
| 2 | 132 | 0.48 | 0.78 | 20 | empty |
| 3 | 139 | 0.48 | 0.78 | 26 | empty |
| 4 | 129 | 0.47 | 0.78 | 23 | empty |
| 5 | 106 | 0.44 | 0.78 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1718 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1585 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1560 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4TM6 · Crystal Structure of EutL from Clostridium Perfringens at 298K · 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 B1BQ33
- Elsewhere: RCSB PDB 4TM6 · PDBe 4TM6 · UniProt B1BQ33
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