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Crystal structure of opuac from B. subtilis in complex with arsenobetaine

Analyse Crystal structure of opuac from B. subtilis in complex with arsenobetaine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NXX
Type: protein
Length: 530 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycine betaine ABC transport system glycine betaine- binding protein opuac
UniProt: A0A085C2M9
Ligands: 3Q7
Pockets: 2 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, D	Glycine betaine ABC transport system glycine betaine- binding protein opuac	protein	265	43% helix, 23% strand	A0A085C2M9

Ligands and binding sites

3Q7 · (trimethylarsonio)acetate · ligand · 2 copies · chains C, D

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.29	0.76	13	empty
2	65	0.29	0.73	15	empty

Interfaces

1 interface between chains.

C–D · 191 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5NXX · Crystal structure of OpuAC from B. subtilis in complex with Arsenobetaine · the same entry in another collection · chain C against C, 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 A0A085C2M9
Elsewhere: RCSB PDB 5NXX · PDBe 5NXX · UniProt A0A085C2M9

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