MolNFT v1 · #181283 · protein

Evolution of a sigma-(C-di-gmp)-antisigma switch

7LQ3 · Rsig: “Evolution of a sigma-(C-di-gmp)-antisigma switch”. X-ray diffraction, 2 ligands (MG, SO4), 1 pocket (best druggability 0.56). MolNFT v1 #181283 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7LQ3
Type: protein
Length: 213 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rsig
UniProt: A0A023X3Z4
Ligands: MG, SO4
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, D	Rsig	protein	71	76% helix, 0% strand	A0A023X3Z4

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains B, A, D
SO4 · Sulfate ion · ion · 2 copies · chains B, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	287	0.56	0.77	27	empty

Interfaces

3 interfaces between chains.

B–A · 1932 Å² buried · 18 hydrogen bonds · protein-protein
A–D · 439 Å² buried · 5 hydrogen bonds · protein-protein
B–D · 218 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

7LQ3 · Evolution of a sigma-(c-di-GMP)-antisigma switch · the same entry in another collection · chain B against B, 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 A0A023X3Z4
Elsewhere: RCSB PDB 7LQ3 · PDBe 7LQ3 · UniProt A0A023X3Z4

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