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Structure of the periplasmic domain of flip

Analyse Structure of the periplasmic domain of flip in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5H72
Type: protein
Length: 536 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar biosynthetic protein flip
UniProt: Q9WZG2
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Flagellar biosynthetic protein flip	protein	67	78% helix, 0% strand	Q9WZG2

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	532	0.71	0.79	59	empty
2	518	0.70	0.79	59	empty
3	395	0.59	0.76	36	empty

Interfaces

11 interfaces between chains.

E–G · 667 Å² buried · 7 hydrogen bonds · protein-protein
F–H · 666 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 663 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 657 Å² buried · 8 hydrogen bonds · protein-protein
E–F · 529 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5H72 · Structure of the periplasmic domain of FliP · 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
Every structure of UniProt Q9WZG2
Elsewhere: RCSB PDB 5H72 · PDBe 5H72 · UniProt Q9WZG2

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