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Crystal structure of bacillus thuringiensis plcr in its apo form

Analyse Crystal structure of bacillus thuringiensis plcr in its apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FSC
Type: protein
Length: 1,058 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional activator plcr protein
UniProt: Q45782
Pockets: 14 · best druggability 0.81

Structure

x-ray diffraction · 3 distinct chains · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional activator plcr protein	protein	264	69% helix, 0% strand	Q45782
B, D	Transcriptional activator plcr protein	protein	264	70% helix, 0% strand	Q45782
C	Transcriptional activator plcr protein	protein	266	68% helix, 0% strand	Q45782

Pockets

14 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	815	0.81	0.83	93	empty
2	386	0.74	0.84	56	empty
3	595	0.71	0.78	64	empty
4	533	0.70	0.79	65	empty
5	267	0.68	0.83	29	empty

Interfaces

4 interfaces between chains.

A–D · 1760 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 1753 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 188 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 186 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4FSC · Crystal Structure of Bacillus thuringiensis PlcR in its apo form · the same entry in another collection · chain D against D, 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 Q45782
Elsewhere: RCSB PDB 4FSC · PDBe 4FSC · UniProt Q45782

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