MolNFT v1 · #118966 · protein

Crystal structure of flid (HAP2) from pseudomonas aeruginosa PAO1

5FHY · B-type flagellar hook-associated protein 2: “Crystal structure of flid (HAP2) from pseudomonas aeruginosa PAO1”. X-ray diffraction, 1 ligand (NA), 1 pocket (best druggability 0.60). MolNFT v1 #118966 on GenesisL1: 3D structure…

PDB: 5FHY
Type: protein
Length: 458 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: B-type flagellar hook-associated protein 2
UniProt: Q9K3C5
Ligands: NA
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	B-type flagellar hook-associated protein 2	protein	229	12% helix, 40% strand	Q9K3C5

Ligands and binding sites

NA · Sodium ion · metal · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	342	0.60	0.77	29	empty

Interfaces

1 interface between chains.

A–B · 305 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5FHY · Crystal structure of FliD (HAP2) from Pseudomonas aeruginosa PAO1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9K3C5 · AlphaFold monomer V2.0 prediction for B-type flagellar hook- associated protein 2 (Q9K3C5) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 Q9K3C5
Elsewhere: RCSB PDB 5FHY · PDBe 5FHY · UniProt Q9K3C5

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