Research workbench

Cryo-EM structure of the flagellar proximal rod with flif peptides from salmonella

Analyse Cryo-EM structure of the flagellar proximal rod with flif peptides from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CG0
Type: protein
Length: 1,487 residues
Chains: 21
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar ms ring L2; Flagellar ms ring L1; Flagellar basal-body rod protein flgc…
UniProt: P15928, P0A1I7, P16437
Pockets: 20 · best druggability 0.72

Structure

electron microscopy · 12 distinct chains · 51% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
0, 1, 2, 3, 4	Flagellar ms ring L2	protein	15	0% helix, 0% strand	—
5, 6, 7, 9, 8	Flagellar ms ring L1	protein	21	0% helix, 10% strand	P15928
f	Flagellar basal-body rod protein flgc	protein	128	47% helix, 20% strand	P0A1I7
g	Flagellar basal-body rod protein flgc	protein	130	49% helix, 18% strand	P0A1I7
h	Flagellar basal-body rod protein flgc	protein	128	44% helix, 15% strand	P0A1I7
j	Flagellar basal-body rod protein flgc	protein	127	48% helix, 17% strand	P0A1I7
l, m	Flagellar basal body rod protein flgb	protein	106	64% helix, 5% strand	P16437
o	Flagellar basal body rod protein flgb	protein	109	63% helix, 5% strand	P16437
p	Flagellar basal-body rod protein flgc	protein	129	47% helix, 18% strand	P0A1I7
i	Flagellar basal-body rod protein flgc	protein	129	44% helix, 16% strand	P0A1I7
k	Flagellar basal body rod protein flgb	protein	108	62% helix, 5% strand	P16437
n	Flagellar basal body rod protein flgb	protein	107	64% helix, 5% strand	P16437

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	960	0.72	0.76	92	empty
2	305	0.64	0.80	35	empty
3	507	0.62	0.75	54	empty
4	252	0.57	0.78	26	empty
5	241	0.56	0.77	23	empty

Interfaces

37 interfaces between chains.

g–p · 1165 Å² buried · 4 hydrogen bonds · protein-protein
i–k · 1096 Å² buried · 6 hydrogen bonds · protein-protein
j–n · 1076 Å² buried · 5 hydrogen bonds · protein-protein
f–l · 1052 Å² buried · 7 hydrogen bonds · protein-protein
h–m · 1044 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7CG0 · Cryo-EM structure of the flagellar proximal rod with FliF peptides from Salmonella · the same entry in another collection · chain 9 against 9, 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 P15928
Every structure of UniProt P0A1I7
Every structure of UniProt P16437
Elsewhere: RCSB PDB 7CG0 · PDBe 7CG0 · UniProt P15928 · UniProt P0A1I7 · UniProt P16437

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.