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Moesin from spodoptera frugiperda reveals the coiled-coil domain at 3.0 ångström resolution

Analyse Moesin from spodoptera frugiperda reveals the coiled-coil domain at 3.0… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2I1K
Type: protein
Length: 545 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Moesin
UniProt: A0T1L9
Ligands: URE, CL
Pockets: 7 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Moesin	protein	545	56% helix, 14% strand	A0T1L9

Ligands and binding sites

URE · Urea · ligand · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	823	0.74	0.79	63	empty
2	604	0.74	0.81	61	empty
3	230	0.69	0.85	25	empty
4	246	0.61	0.81	38	empty
5	151	0.46	0.76	20	empty

Compared structures

2I1K · Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom… · the same entry in another collection · 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 A0T1L9
Elsewhere: RCSB PDB 2I1K · PDBe 2I1K · UniProt A0T1L9

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