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Crystal structure of the cytoplasmic domain of flha in monomeric form

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

PDB: 6CH1
Type: protein
Length: 332 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar biosynthesis protein flha
UniProt: P40729
Pockets: 4 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar biosynthesis protein flha	protein	332	48% helix, 18% strand	P40729

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 9 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	146	0.45	0.76	28	EDO
2	144	0.44	0.76	22	empty
3	72	0.39	0.78	20	EDO
4	64	0.34	0.76	14	empty

Compared structures

6CH1 · Crystal structure of the cytoplasmic domain of FlhA in monomeric form · 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

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
Elsewhere: RCSB PDB 6CH1 · PDBe 6CH1 · UniProt P40729

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