Research workbench
Crystal structure of the SAMD1 SAM domain in another crystal form
Analyse Crystal structure of the SAMD1 SAM domain in another crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LUK
- Type
- protein
- Length
- 1,380 residues
- Chains
- 20
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Atherin
- UniProt
- Q6SPF0
- Ligands
- SO4
- Pockets
- 16 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T | Atherin | protein | 69 | 71% helix, 0% strand | Q6SPF0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 18 copies · chains A, B, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 709 | 0.78 | 0.83 | 69 | empty |
| 2 | 701 | 0.78 | 0.83 | 65 | empty |
| 3 | 228 | 0.65 | 0.84 | 27 | empty |
| 4 | 205 | 0.63 | 0.83 | 24 | empty |
| 5 | 203 | 0.63 | 0.83 | 25 | empty |
Interfaces
42 interfaces between chains.
- L–O · 546 Ų buried · 10 hydrogen bonds · protein-protein
- F–J · 544 Ų buried · 12 hydrogen bonds · protein-protein
- K–O · 542 Ų buried · 12 hydrogen bonds · protein-protein
- B–E · 542 Ų buried · 11 hydrogen bonds · protein-protein
- R–S · 532 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6LUK · Crystal structure of the SAMD1 SAM domain in another crystal form · the same entry in another collection · chain T against T, 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 Q6SPF0
- Elsewhere: RCSB PDB 6LUK · PDBe 6LUK · UniProt Q6SPF0
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