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Crystal structure of the cytoplasmic domain of flha and flit-flid complex

Analyse Crystal structure of the cytoplasmic domain of flha and flit-flid complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CH2
Type: protein
Length: 1,426 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar biosynthesis protein flha; Flagellar hook-associated protein 2,FLAGELLAR…
UniProt: P40729, P16328, P0A1N3
Pockets: 15 · best druggability 0.75

Structure

x-ray diffraction · 6 distinct chains · 58% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar biosynthesis protein flha	protein	331	46% helix, 19% strand	P40729
B	Flagellar biosynthesis protein flha	protein	332	46% helix, 19% strand	P40729
C	Flagellar biosynthesis protein flha	protein	329	47% helix, 19% strand	P40729
D	Flagellar hook-associated protein 2,FLAGELLAR protein flit	protein	144	87% helix, 0% strand	P16328, P0A1N3
E	Flagellar hook-associated protein 2,FLAGELLAR protein flit	protein	147	86% helix, 0% strand	P16328, P0A1N3
F	Flagellar hook-associated protein 2,FLAGELLAR protein flit	protein	143	80% helix, 0% strand	P16328, P0A1N3

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	430	0.75	0.85	52	empty
2	453	0.72	0.82	43	empty
3	211	0.68	0.86	42	empty
4	627	0.68	0.77	65	empty
5	337	0.64	0.79	42	empty

Interfaces

8 interfaces between chains.

C–F · 988 Å² buried · 9 hydrogen bonds · protein-protein
B–E · 740 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 686 Å² buried · 6 hydrogen bonds · protein-protein
B–F · 683 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 660 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6CH2 · Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex · the same entry in another collection · chain A against A, TM-score 1.00
P40729 · AlphaFold monomer V2.0 prediction for flagellar biosynthesis protein flha (P40729) · a predicted model of the same protein · chain A against A, TM-score 0.99
P0A1N3 · AlphaFold monomer V2.0 prediction for flagellar protein flit (P0A1N3) · a predicted model of the same protein · chain D against A, TM-score 0.68

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 P40729
Every structure of UniProt P16328
Every structure of UniProt P0A1N3
Elsewhere: RCSB PDB 6CH2 · PDBe 6CH2 · UniProt P40729 · UniProt P16328 · UniProt P0A1N3

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