MolNFT v1 · #105125 · protein + RNA

E.COLI hfq in complex with RNA aus

4QVC · RNA-binding protein hfq: “E.COLI hfq in complex with RNA aus”. X-ray diffraction, 1 pocket (best druggability 0.71). MolNFT v1 #105125 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4QVC
Type: protein + RNA
Length: 367 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-binding protein hfq; RNA (5'-R(*AP*U*AP*AP*CP*UP*A)-3')
UniProt: C1IFD2
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 22% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E	RNA-binding protein hfq	protein	60	22% helix, 50% strand	C1IFD2
C	RNA-binding protein hfq	protein	63	22% helix, 48% strand	C1IFD2
F	RNA-binding protein hfq	protein	61	23% helix, 51% strand	C1IFD2
G	RNA (5'-R(APUAPAPCPUP*A)-3')	rna	3	—	—

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	953	0.71	0.75	62	empty

Interfaces

8 interfaces between chains.

C–D · 771 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 678 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 676 Å² buried · 9 hydrogen bonds · protein-protein
A–F · 673 Å² buried · 11 hydrogen bonds · protein-protein
E–F · 671 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4QVC · E.coli Hfq in complex with RNA Aus · 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 C1IFD2
Elsewhere: RCSB PDB 4QVC · PDBe 4QVC · UniProt C1IFD2

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