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Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E. COLI ammonia channel amtb

Analyse Substrate binding, deprotonation and selectivity at the periplasmic entrance of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3C1I
Type: protein
Length: 366 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ammonia channel
UniProt: P69681
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ammonia channel	protein	366	74% helix, 2% strand	P69681

Ligands and binding sites

ACT · Acetate ion · additive · chains A
LDA · Lauryl dimethylamine-N-oxide · 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	173	0.68	0.86	38	LDA
2	170	0.46	0.75	25	ACT

Compared structures

3C1I · Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E.… · 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 3C1I · PDBe 3C1I · UniProt P69681

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