MolNFT v1 · #106009 · protein

Crystal structure of the ferm domain of human ezrin

4RMA: “Crystal structure of the ferm domain of human ezrin”. X-ray diffraction, 1 ligand (SO4), 10 pockets (best druggability 0.76). MolNFT v1 #106009 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4RMA
Type: protein
Length: 580 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ezrin
UniProt: P15311
Ligands: SO4
Pockets: 10 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ezrin	protein	295	38% helix, 25% strand	P15311
B	Ezrin	protein	285	39% helix, 25% strand	P15311

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1187	0.76	0.78	120	SO4
2	404	0.62	0.77	46	empty
3	381	0.61	0.77	44	empty
4	99	0.42	0.78	17	empty
5	61	0.41	0.81	21	empty

Interfaces

1 interface between chains.

A–B · 940 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

4RMA · Crystal structure of the FERM domain of human ezrin · the same entry in another collection · chain A against A, TM-score 1.00
P15311 · AlphaFold monomer V2.0 prediction for ezrin (P15311) · a predicted model of the same protein · chain B 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 P15311
Elsewhere: RCSB PDB 4RMA · PDBe 4RMA · UniProt P15311

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