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Structure of the bacterial acetate channel satp

Analyse Structure of the bacterial acetate channel satp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZUG
Type: protein
Length: 1,090 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P0AC98
Ligands: BNG

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E	—	protein	182	—	P0AC98
C, F	—	protein	181	—	P0AC98

Ligands and binding sites

BNG · nonyl beta-D-glucopyranoside · ligand · 3 copies · chains A, C, F, B, E

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

Compared structures

5ZUG · Structure of the bacterial acetate channel SatP · the same entry in another collection · chain F against F, TM-score 1.00
P0AC98 · AlphaFold monomer V2.0 prediction for succinate-ACETATE/PROTON symporter satp (P0AC98) · a predicted model of the same protein · chain A against A, 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 P0AC98
Elsewhere: RCSB PDB 5ZUG · PDBe 5ZUG · UniProt P0AC98

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