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Crystal structure of the flagellar assembly factor fliw

Analyse Crystal structure of the flagellar assembly factor fliw in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DMD
Type: protein
Length: 285 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar assembly factor fliw
UniProt: A4ISV0
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar assembly factor fliw	protein	144	13% helix, 31% strand	A4ISV0
B	Flagellar assembly factor fliw	protein	141	13% helix, 31% strand	A4ISV0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	270	0.56	0.77	45	empty
2	63	0.28	0.72	13	empty

Interfaces

1 interface between chains.

A–B · 312 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5DMD · Crystal structure of the flagellar assembly factor FliW · the same entry in another collection · chain B against B, TM-score 1.00
A4ISV0 · AlphaFold monomer V2.0 prediction for flagellar assembly factor fliw (A4ISV0) · a predicted model of the same protein · chain B 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 A4ISV0
Elsewhere: RCSB PDB 5DMD · PDBe 5DMD · UniProt A4ISV0

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