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The mechanism of ammonia transport based on the crystal structure of amtb of E. COLI.

Analyse The mechanism of ammonia transport based on the crystal structure of amtb of E.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XQE
Type: protein
Length: 366 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable ammonium transporter
UniProt: P69681
Ligands: SO4
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable ammonium transporter	protein	366	75% helix, 2% strand	P69681

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A
ACT · Acetate ion · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	120	0.51	0.80	34	empty
2	167	0.48	0.76	27	ACT

Compared structures

1XQE · The mechanism of ammonia transport based on the crystal structure of AmtB of E. coli. · the same entry in another collection · chain A against A, TM-score 1.00
P69681 · AlphaFold monomer V2.0 prediction for ammonia channel (P69681) · a predicted model of the same protein · chain A against A, TM-score 0.99

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
Elsewhere: RCSB PDB 1XQE · PDBe 1XQE · UniProt P69681

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