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Crystal structure of the moesin ferm DOMAIN/TAIL domain complex

Analyse Crystal structure of the moesin ferm DOMAIN/TAIL domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EF1
Type: protein
Length: 768 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Moesin
UniProt: P26038
Ligands: SO4
Pockets: 15 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Moesin	protein	294	38% helix, 26% strand	P26038
C, D	Moesin	protein	90	57% helix, 1% strand	P26038

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	761	0.77	0.81	82	empty
2	68	0.72	0.97	24	empty
3	521	0.72	0.80	41	empty
4	374	0.71	0.83	40	empty
5	362	0.65	0.79	35	empty

Interfaces

6 interfaces between chains.

A–C · 2564 Å² buried · 41 hydrogen bonds · protein-protein
B–D · 2559 Å² buried · 43 hydrogen bonds · protein-protein
C–D · 370 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 215 Å² buried · 1 hydrogen bond · protein-protein
C–B · 109 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

1EF1 · Crystal structure of the moesin ferm DOMAIN/TAIL domain complex · the same entry in another collection · chain A against A, TM-score 1.00
P26038 · AlphaFold monomer V2.0 prediction for moesin (P26038) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P26038
Elsewhere: RCSB PDB 1EF1 · PDBe 1EF1 · UniProt P26038

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