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Crystal structure of escherichia COLI hfq surface mutant

Analyse Crystal structure of escherichia COLI hfq surface mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JRK
Type: protein
Length: 192 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein hfq
UniProt: P0A6X3
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 3 distinct chains · 21% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein hfq	protein	64	20% helix, 48% strand	P0A6X3
B	Protein hfq	protein	66	21% helix, 47% strand	P0A6X3
C	Protein hfq	protein	62	21% helix, 50% strand	P0A6X3

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	144	0.45	0.76	25	empty

Interfaces

2 interfaces between chains.

A–B · 793 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 747 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4JRK · Crystal Structure of Escherichia coli Hfq Surface Mutant · the same entry in another collection · chain A against A, TM-score 1.00
P0A6X3 · AlphaFold monomer V2.0 prediction for RNA-binding protein hfq (P0A6X3) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 4JRK · PDBe 4JRK · UniProt P0A6X3

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