MolNFT v1 · #142851 · protein

Structure of the 40-167 fragment of flil

6AHQ · Flagellar protein flil: “Structure of the 40-167 fragment of flil”. X-ray diffraction, 20 pockets (best druggability 0.52). MolNFT v1 #142851 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6AHQ
Type: protein
Length: 2,146 residues
Chains: 20
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar protein flil
Pockets: 20 · best druggability 0.52

Structure

x-ray diffraction · 3 distinct chains · 46% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E, F, J, P	Flagellar protein flil	protein	108	44% helix, 26% strand	—
C, G, H, I, K, L, M, O, Q, R, S, T	Flagellar protein flil	protein	107	47% helix, 29% strand	—
N	Flagellar protein flil	protein	106	46% helix, 31% strand	—

Pockets

20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	65	0.52	0.86	17	empty
2	59	0.51	0.87	17	empty
3	296	0.51	0.73	27	empty
4	68	0.50	0.85	16	empty
5	77	0.50	0.84	18	empty

Interfaces

30 interfaces between chains.

A–J · 882 Å² buried · 11 hydrogen bonds · protein-protein
H–I · 847 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 841 Å² buried · 8 hydrogen bonds · protein-protein
F–G · 830 Å² buried · 8 hydrogen bonds · protein-protein
E–F · 815 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6AHQ · Structure of the 40-167 fragment of FliL · 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
Elsewhere: RCSB PDB 6AHQ · PDBe 6AHQ

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