Research workbench
Regulating the escherichia COLI ammonia channel: the crystal structure of the amtb-glnk complex
Analyse Regulating the escherichia COLI ammonia channel: the crystal structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NUU
- Type
- protein
- Length
- 3,127 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ammonia channel; Nitrogen regulatory protein P-II 2
- UniProt
- P69681, P0AC55
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 3 distinct chains · 65% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, F | Ammonia channel | protein | 409 | 71% helix, 2% strand | P69681 |
| D | Ammonia channel | protein | 410 | 70% helix, 2% strand | P69681 |
| G, H, I, J, K, L | Nitrogen regulatory protein P-II 2 | protein | 112 | 26% helix, 38% strand | P0AC55 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 935 | 0.88 | 0.90 | 117 | ADP |
| 2 | 715 | 0.87 | 0.90 | 98 | ADP |
| 3 | 865 | 0.84 | 0.87 | 123 | empty |
| 4 | 539 | 0.83 | 0.89 | 75 | empty |
| 5 | 203 | 0.79 | 0.93 | 29 | empty |
Interfaces
32 interfaces between chains.
- E–F · 2106 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 2096 Ų buried · 15 hydrogen bonds · protein-protein
- D–F · 2088 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 2080 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 2078 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2NUU · Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK… · the same entry in another collection · chain L against L, 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 P69681
- Every structure of UniProt P0AC55
- Elsewhere: RCSB PDB 2NUU · PDBe 2NUU · UniProt P69681 · UniProt P0AC55
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