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Structure of the 328-692 fragment of flha (D456V)

Analyse Structure of the 328-692 fragment of flha (D456V) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AI1
Type: protein
Length: 690 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar biosynthesis protein flha
UniProt: P40729
Pockets: 11 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Flagellar biosynthesis protein flha	protein	345	46% helix, 17% strand	P40729

Pockets

11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	578	0.65	0.76	47	empty
2	240	0.54	0.77	33	empty
3	118	0.47	0.79	17	empty
4	150	0.45	0.77	21	empty
5	141	0.43	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 1487 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

6AI1 · Structure of the 328-692 fragment of FlhA (D456V) · 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 0.93

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 6AI1 · PDBe 6AI1 · UniProt P40729

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