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Crystal structure of hfq riboregulator from E. COLI (P1 space group)

Analyse Crystal structure of hfq riboregulator from E. COLI (P1 space group) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YHT
Type: protein
Length: 756 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein hfq
UniProt: P0A6X3
Pockets: 9 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Protein hfq	protein	63	21% helix, 48% strand	P0A6X3

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	803	0.82	0.85	52	empty
2	821	0.75	0.79	73	empty
3	263	0.73	0.87	40	empty
4	391	0.72	0.83	47	empty
5	210	0.69	0.86	32	empty

Interfaces

26 interfaces between chains.

K–L · 765 Å² buried · 12 hydrogen bonds · protein-protein
D–E · 758 Å² buried · 11 hydrogen bonds · protein-protein
G–L · 753 Å² buried · 11 hydrogen bonds · protein-protein
I–J · 750 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 747 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2YHT · Crystal structure of Hfq riboregulator from E. coli (P1 space group) · the same entry in another collection · chain L against L, 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 P0A6X3
Elsewhere: RCSB PDB 2YHT · PDBe 2YHT · UniProt P0A6X3

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