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Crystal structure of the first two domains of the initiation module of lgra

Analyse Crystal structure of the first two domains of the initiation module of lgra in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ES6
Type: protein
Length: 583 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Linear gramicidin synthase subunit a
UniProt: Q70LM7
Pockets: 5 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Linear gramicidin synthase subunit a	protein	583	31% helix, 25% strand	Q70LM7

Ligands and binding sites

FMT · Formic acid · additive · 3 copies · chains A

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	359	0.71	0.83	43	FMT
2	374	0.60	0.76	49	empty
3	96	0.42	0.78	21	empty
4	83	0.40	0.78	16	empty
5	129	0.36	0.73	26	empty

Compared structures

5ES6 · Crystal structure of the first two domains of the initiation module of LgrA · the same entry in another collection · chain A against A, TM-score 1.00
Q70LM7 · AlphaFold monomer V2.0 prediction for linear gramicidin synthase subunit a (Q70LM7) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q70LM7
Elsewhere: RCSB PDB 5ES6 · PDBe 5ES6 · UniProt Q70LM7

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