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Conformational plasticity of the coiled coil domain of bmrr is required for bmr promoter binding-the unliganded structure of bmrr

Analyse Conformational plasticity of the coiled coil domain of bmrr is required for bmr… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IAO
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Multidrug-efflux transporter 1 regulator
UniProt: P39075
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Multidrug-efflux transporter 1 regulator	protein	273	40% helix, 22% strand	P39075

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	150	0.56	0.81	26	empty
2	184	0.52	0.78	30	empty

Compared structures

3IAO · Conformational plasticity of the coiled coil domain of BmrR is required for bmr promoter… · the same entry in another collection · chain A against A, TM-score 1.00
P39075 · AlphaFold monomer V2.0 prediction for multidrug-efflux transporter 1 regulator (P39075) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P39075
Elsewhere: RCSB PDB 3IAO · PDBe 3IAO · UniProt P39075

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