MolNFT v1 · #112056 · protein
Asp-tar from E. COLI
4Z9H · Methyl-accepting chemotaxis protein II: “Asp-tar from E. COLI”. X-ray diffraction, 1 ligand (ASP), 3 pockets (best druggability 0.68). MolNFT v1 #112056 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4Z9H
- Type
- protein
- Length
- 323 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein II
- UniProt
- P07017
- Ligands
- ASP
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein II | protein | 165 | 79% helix, 0% strand | P07017 |
| B | Methyl-accepting chemotaxis protein II | protein | 158 | 85% helix, 0% strand | P07017 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 575 | 0.68 | 0.77 | 55 | empty |
| 2 | 57 | 0.47 | 0.85 | 15 | empty |
| 3 | 56 | 0.34 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1555 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
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 P07017
- Elsewhere: RCSB PDB 4Z9H · PDBe 4Z9H · UniProt P07017
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