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Crystal structure of human mxb stalk domain

Analyse Crystal structure of human mxb stalk domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4X0R
Type: protein
Length: 417 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interferon-induced GTP-binding protein MX2
UniProt: P20592
Pockets: 5 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Interferon-induced GTP-binding protein MX2	protein	216	87% helix, 0% strand	P20592
A	Interferon-induced GTP-binding protein MX2	protein	201	83% helix, 0% strand	P20592

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	443	0.63	0.76	37	empty
2	186	0.50	0.76	22	empty
3	112	0.45	0.78	17	empty
4	120	0.45	0.77	18	empty
5	59	0.39	0.80	16	empty

Interfaces

1 interface between chains.

B–A · 1099 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4X0R · Crystal structure of human MxB stalk domain · the same entry in another collection · chain B against B, TM-score 1.00
P20592 · AlphaFold monomer V2.0 prediction for interferon-induced GTP-binding protein MX2 (P20592) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P20592
Elsewhere: RCSB PDB 4X0R · PDBe 4X0R · UniProt P20592

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