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Structure of the sensor domain (short construct) of the anti-sigma factor RSGI4 in pseudobacteroides cellulosolvens

Analyse Structure of the sensor domain (short construct) of the anti-sigma factor RSGI4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CG8
Type: protein
Length: 415 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anti-sigma factor rsgi, N-terminal
UniProt: A0A0L6JMH4
Ligands: PEU
Pockets: 5 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Anti-sigma factor rsgi, N-terminal	protein	105	3% helix, 51% strand	A0A0L6JMH4
C	Anti-sigma factor rsgi, N-terminal	protein	100	0% helix, 54% strand	A0A0L6JMH4

Ligands and binding sites

PEU · 2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56, 59,62,65,68,71,74,77,80-heptacosaoxadooctacontan-82-ol · ligand · 2 copies · chains A, B, C, D
ACT · Acetate ion · additive · 3 copies · chains A, B, C, D

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

Pockets

5 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	989	0.85	0.85	87	PEU
2	367	0.66	0.79	30	empty
3	88	0.46	0.81	23	empty
4	65	0.38	0.79	14	empty
5	61	0.34	0.77	15	empty

Interfaces

6 interfaces between chains.

A–D · 765 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 654 Å² buried · 9 hydrogen bonds · protein-protein
C–D · 634 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 566 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 366 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7CG8 · Structure of the sensor domain (short construct) of the anti-sigma factor RsgI4 in… · 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 A0A0L6JMH4
Elsewhere: RCSB PDB 7CG8 · PDBe 7CG8 · UniProt A0A0L6JMH4

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