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Crystal structure of fbf-2 repeat 5 mutant (C363A, R364Y) in complex with 8-nt RNA

Analyse Crystal structure of fbf-2 repeat 5 mutant (C363A, R364Y) in complex with 8-nt… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NOC
Type: protein + RNA
Length: 410 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fem-3 mRNA-binding factor 2; RNA (5'-R(*UP*GP*UP*AP*AP*AP*UP*A)-3')
UniProt: Q09312
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fem-3 mRNA-binding factor 2	protein	402	71% helix, 1% strand	Q09312
B	RNA (5'-R(UPGPUPAPAPAPUPA)-3')	rna	8	—	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.37	0.79	15	empty
2	53	0.30	0.76	11	empty

Interfaces

1 interface between chains.

A–B · 1431 Å² buried · 44 hydrogen bonds · protein-nucleic

Compared structures

6NOC · Crystal structure of FBF-2 repeat 5 mutant (C363A, R364Y) in complex with 8-nt RNA · the same entry in another collection · chain A against A, TM-score 1.00
Q09312 · AlphaFold monomer V2.0 prediction for fem-3 mRNA-binding factor 2 (Q09312) · a predicted model of the same protein · 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 Q09312
Elsewhere: RCSB PDB 6NOC · PDBe 6NOC · UniProt Q09312

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