Research workbench
Monoclinic eutl - structure determined from merged "group 2" data
Analyse Monoclinic eutl - structure determined from merged "group 2" data in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ARD
- Type
- protein
- Length
- 653 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ethanolamine utilization protein
- UniProt
- A0A174CSE0
- Ligands
- NA
- Pockets
- 6 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ethanolamine utilization protein | protein | 217 | 35% helix, 28% strand | A0A174CSE0 |
| B, C | Ethanolamine utilization protein | protein | 218 | 36% helix, 28% strand | A0A174CSE0 |
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
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.50 | 0.79 | 25 | empty |
| 2 | 116 | 0.49 | 0.80 | 24 | empty |
| 3 | 118 | 0.47 | 0.79 | 22 | empty |
| 4 | 143 | 0.47 | 0.77 | 29 | empty |
| 5 | 131 | 0.45 | 0.77 | 23 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1565 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1564 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1557 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6ARD · Monoclinic EutL - structure determined from merged Group 2" data" · 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 A0A174CSE0
- Elsewhere: RCSB PDB 6ARD · PDBe 6ARD · UniProt A0A174CSE0
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