MolNFT v1 · #46118 · protein

Regulating the escherichia COLI ammonia channel: the crystal structure of the amtb-glnk complex

2NUU: “Regulating the escherichia COLI ammonia channel: the crystal structure of the amtb-glnk complex”. X-ray diffraction, 1 ligand (ADP), 20 pockets (best druggability 0.88). MolNFT v1 #46118 on GenesisL1: 3D structure, binding sites and…

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.

Pocket	Volume (Å³)	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 Å² buried · 12 hydrogen bonds · protein-protein
D–E · 2096 Å² buried · 15 hydrogen bonds · protein-protein
D–F · 2088 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 2080 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 2078 Å² 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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