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Crystal structure of response regulator (signal receiver domain) from bermanella marisrubri

Analyse Crystal structure of response regulator (signal receiver domain) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LTE
Type: protein
Length: 2,873 residues
Chains: 24
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Response regulator
UniProt: Q1N036
Ligands: PO4
Pockets: 20 · best druggability 0.69

Structure

x-ray diffraction · 10 distinct chains · 46% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Response regulator	protein	118	45% helix, 21% strand	Q1N036
B, J, K, S, W	Response regulator	protein	120	46% helix, 21% strand	Q1N036
C, N, T	Response regulator	protein	119	45% helix, 21% strand	Q1N036
D, E, F, H, P	Response regulator	protein	123	47% helix, 20% strand	Q1N036
G	Response regulator	protein	121	45% helix, 21% strand	Q1N036
I	Response regulator	protein	119	48% helix, 22% strand	Q1N036
L, M, R, V, X	Response regulator	protein	118	46% helix, 21% strand	Q1N036
O	Response regulator	protein	117	46% helix, 21% strand	Q1N036
Q	Response regulator	protein	117	46% helix, 18% strand	Q1N036
U	Response regulator	protein	119	45% helix, 19% strand	Q1N036

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains F, L, T
GOL · Glycerol · additive · chains R, S

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	311	0.69	0.83	53	empty
2	292	0.69	0.84	41	empty
3	392	0.69	0.81	58	empty
4	493	0.68	0.79	75	empty
5	384	0.65	0.79	53	empty

Interfaces

43 interfaces between chains.

I–J · 868 Å² buried · 7 hydrogen bonds · protein-protein
U–V · 855 Å² buried · 4 hydrogen bonds · protein-protein
W–X · 847 Å² buried · 6 hydrogen bonds · protein-protein
M–N · 837 Å² buried · 5 hydrogen bonds · protein-protein
K–L · 832 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3LTE · CRYSTAL STRUCTURE OF RESPONSE REGULATOR (SIGNAL RECEIVER DOMAIN) FROM Bermanella… · 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 Q1N036
Elsewhere: RCSB PDB 3LTE · PDBe 3LTE · UniProt Q1N036

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