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H57T hfq from pseudomonas aeruginosa

Analyse H57T hfq from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3INZ
Type: protein
Length: 408 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein hfq
UniProt: Q9HUM0
Ligands: CD, NA, CL
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 5 distinct chains · 19% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein hfq	protein	69	19% helix, 42% strand	Q9HUM0
B, D	Protein hfq	protein	67	19% helix, 45% strand	Q9HUM0
C	Protein hfq	protein	66	20% helix, 45% strand	Q9HUM0
E	Protein hfq	protein	68	19% helix, 44% strand	Q9HUM0
F	Protein hfq	protein	71	18% helix, 44% strand	Q9HUM0

Ligands and binding sites

CD · Cadmium ion · metal · 9 copies · chains A, B, C, D, E, F
NA · Sodium ion · metal · chains A, B
CL · Chloride ion · ion · chains C, D

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	904	0.72	0.76	67	CD

Interfaces

6 interfaces between chains.

A–F · 905 Å² buried · 16 hydrogen bonds · protein-protein
D–E · 837 Å² buried · 12 hydrogen bonds · protein-protein
E–F · 779 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 773 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 764 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3INZ · H57T Hfq from Pseudomonas aeruginosa · the same entry in another collection · chain F against F, TM-score 1.00
Q9HUM0 · AlphaFold monomer V2.0 prediction for RNA-binding protein hfq (Q9HUM0) · 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 Q9HUM0
Elsewhere: RCSB PDB 3INZ · PDBe 3INZ · UniProt Q9HUM0

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