MolNFT v1 · #141782 · protein

Crystal structure of bacillus cereus flgl

5ZIY · Flagellar hook-associated protein 3: “Crystal structure of bacillus cereus flgl”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.52). MolNFT v1 #141782 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5ZIY
Type: protein
Length: 368 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar hook-associated protein 3
UniProt: A0A164TZ51
Ligands: ZN
Pockets: 4 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar hook-associated protein 3	protein	195	70% helix, 9% strand	A0A164TZ51
B	Flagellar hook-associated protein 3	protein	173	66% helix, 10% strand	A0A164TZ51

Ligands and binding sites

ZN · Zinc ion · metal · 7 copies · chains A, B

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

Pockets

4 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	53	0.52	0.87	16	empty
2	85	0.44	0.80	19	empty
3	126	0.41	0.75	19	empty
4	80	0.40	0.78	16	empty

Interfaces

1 interface between chains.

A–B · 961 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5ZIY · Crystal structure of Bacillus cereus FlgL · 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 A0A164TZ51
Elsewhere: RCSB PDB 5ZIY · PDBe 5ZIY · UniProt A0A164TZ51

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