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Structure of the arginine repressor from bacillus stearothermophilus

Analyse Structure of the arginine repressor from bacillus stearothermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B4A
Type: protein
Length: 876 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arginine repressor
UniProt: O31408
Pockets: 10 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Arginine repressor	protein	146	46% helix, 23% strand	O31408

Pockets

10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	934	0.85	0.86	88	empty
2	304	0.79	0.90	37	empty
3	308	0.74	0.86	31	empty
4	96	0.59	0.87	17	empty
5	87	0.57	0.87	17	empty

Interfaces

14 interfaces between chains.

A–F · 981 Å² buried · 7 hydrogen bonds · protein-protein
B–E · 864 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 862 Å² buried · 7 hydrogen bonds · protein-protein
D–E · 529 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 471 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1B4A · Structure of the arginine repressor from bacillus stearothermophilus · the same entry in another collection · chain C against C, TM-score 1.00
O31408 · AlphaFold monomer V2.0 prediction for arginine repressor (O31408) · a predicted model of the same protein · chain A against A, TM-score 0.71

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 O31408
Elsewhere: RCSB PDB 1B4A · PDBe 1B4A · UniProt O31408

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