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Crystal structure of fbf-2/FEM-3 pme complex

Analyse Crystal structure of fbf-2/FEM-3 pme complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K64
Type: protein + RNA
Length: 409 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fem-3 mRNA-binding factor 2; 5'-R(*UP*GP*UP*GP*UP*CP*AP*UP*U)-3'
UniProt: Q09312
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fem-3 mRNA-binding factor 2	protein	400	72% helix, 2% strand	Q09312
B	5'-R(UPGPUPGPUPCPAPUP*U)-3'	rna	9	—	—

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	64	0.35	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 1299 Å² buried · 32 hydrogen bonds · protein-nucleic

Compared structures

3K64 · Crystal structure of FBF-2/fem-3 PME complex · the same entry in another collection · chain B against B, 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 3K64 · PDBe 3K64 · UniProt Q09312

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