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Structure of bacterial flagellar capping protein flid

Analyse Structure of bacterial flagellar capping protein flid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SIH
Type: protein
Length: 4,880 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar hook-associated protein 2
UniProt: A0A3I4YJR7
Pockets: 20 · best druggability 0.72

Structure

electron microscopy · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, H, B, F, C, G, D, I, E, J	Flagellar hook-associated protein 2	protein	488	42% helix, 19% strand	A0A3I4YJR7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.72	0.97	19	empty
2	68	0.72	0.96	19	empty
3	68	0.71	0.96	19	empty
4	71	0.71	0.95	19	empty
5	66	0.70	0.95	18	empty

Interfaces

40 interfaces between chains.

A–G · 1169 Å² buried · 2 hydrogen bonds · protein-protein
C–I · 1162 Å² buried · 2 hydrogen bonds · protein-protein
F–D · 1155 Å² buried · 2 hydrogen bonds · protein-protein
B–J · 1143 Å² buried · 2 hydrogen bonds · protein-protein
H–E · 1143 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6SIH · Structure of bacterial flagellar capping protein FliD · 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 A0A3I4YJR7
Elsewhere: RCSB PDB 6SIH · PDBe 6SIH · UniProt A0A3I4YJR7

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