Research workbench

Beryllium fluorinated receiver domain of bfmr from acinetobacter baumannii

Analyse Beryllium fluorinated receiver domain of bfmr from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BR7
Type: protein
Length: 246 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bfmr
UniProt: Q2VSW6
Ligands: BEF, MG
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bfmr	protein	121	47% helix, 19% strand	Q2VSW6
B	Bfmr	protein	125	45% helix, 18% strand	Q2VSW6

Ligands and binding sites

BEF · Beryllium trifluoride ion · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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	217	0.51	0.76	27	empty
2	69	0.43	0.80	18	empty

Interfaces

1 interface between chains.

A–B · 1051 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

6BR7 · Beryllium fluorinated receiver domain of BfmR from Acinetobacter baumannii · the same entry in another collection · 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 Q2VSW6
Elsewhere: RCSB PDB 6BR7 · PDBe 6BR7 · UniProt Q2VSW6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.