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Modified human mxa, nucleotide-free form

Analyse Modified human mxa, nucleotide-free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GTM
Type: protein
Length: 1,042 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interferon-induced GTP-binding protein MX1
UniProt: P20591
Pockets: 14 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 63% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Interferon-induced GTP-binding protein MX1	protein	520	64% helix, 9% strand	P20591
B	Interferon-induced GTP-binding protein MX1	protein	522	63% helix, 8% strand	P20591

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	625	0.74	0.81	55	empty
2	266	0.65	0.82	34	empty
3	66	0.62	0.91	19	empty
4	329	0.61	0.78	47	empty
5	231	0.55	0.78	36	empty

Interfaces

1 interface between chains.

A–B · 984 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5GTM · Modified human MxA, nucleotide-free form · the same entry in another collection · chain A against A, TM-score 1.00
P20591 · AlphaFold monomer V2.0 prediction for interferon-induced GTP-binding protein MX1 (P20591) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P20591
Elsewhere: RCSB PDB 5GTM · PDBe 5GTM · UniProt P20591

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