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1.55 a crystal structure of the pleiotropic translational regulator, hfq

Analyse 1.55 a crystal structure of the pleiotropic translational regulator, hfq in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KQ1
Type: protein
Length: 734 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Host factor for Q beta
UniProt: Q99UG9
Pockets: 12 · best druggability 0.90

Structure

x-ray diffraction · 3 distinct chains · 24% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, I, Y	Host factor for Q beta	protein	60	25% helix, 53% strand	Q99UG9
B, K, M, S, T, N, R, W	Host factor for Q beta	protein	61	25% helix, 52% strand	Q99UG9
H	Host factor for Q beta	protein	66	21% helix, 50% strand	Q99UG9

Ligands and binding sites

ACY · Acetic acid · additive · 5 copies · chains A, H, I, S, T, R, W

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1168	0.90	0.92	153	ACY
2	470	0.83	0.90	68	ACY
3	1118	0.82	0.83	57	empty
4	74	0.58	0.89	19	empty
5	272	0.48	0.73	38	ACY

Interfaces

25 interfaces between chains.

I–K · 762 Å² buried · 14 hydrogen bonds · protein-protein
Y–N · 762 Å² buried · 11 hydrogen bonds · protein-protein
K–M · 744 Å² buried · 16 hydrogen bonds · protein-protein
A–H · 737 Å² buried · 9 hydrogen bonds · protein-protein
S–T · 729 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1KQ1 · 1.55 A Crystal structure of the pleiotropic translational regulator, Hfq · 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 Q99UG9
Elsewhere: RCSB PDB 1KQ1 · PDBe 1KQ1 · UniProt Q99UG9

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