MolNFT v1 · #152648 · protein
The ligand binding domain of MLP24 with asparagine
6IOR · Methyl-accepting chemotaxis protein: “The ligand binding domain of MLP24 with asparagine”. X-ray diffraction, 2 ligands (ASN, CA), 11 pockets (best druggability 0.78). MolNFT v1 #152648 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6IOR
- Type
- protein
- Length
- 962 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein
- UniProt
- A0A0H6VSA0
- Ligands
- ASN, CA
- Pockets
- 11 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Methyl-accepting chemotaxis protein | protein | 241 | 38% helix, 29% strand | A0A0H6VSA0 |
| C, D | Methyl-accepting chemotaxis protein | protein | 240 | 37% helix, 29% strand | A0A0H6VSA0 |
Ligands and binding sites
- ASN · Asparagine · ligand · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.78 | 0.98 | 19 | empty |
| 2 | 96 | 0.78 | 0.98 | 19 | empty |
| 3 | 946 | 0.70 | 0.75 | 87 | empty |
| 4 | 316 | 0.57 | 0.76 | 34 | empty |
| 5 | 282 | 0.52 | 0.75 | 38 | empty |
Interfaces
4 interfaces between chains.
- A–C · 864 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 848 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 675 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 659 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6IOR · The ligand binding domain of Mlp24 with asparagine · the same entry in another collection · chain B against B, 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 A0A0H6VSA0
- Elsewhere: RCSB PDB 6IOR · PDBe 6IOR · UniProt A0A0H6VSA0
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