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Crystal structure of human FE65 ww domain

Analyse Crystal structure of human FE65 ww domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IDH
Type: protein
Length: 249 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amyloid beta A4 protein-binding family B member 1
UniProt: O00213
Ligands: SO4
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 4 distinct chains · 0% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, F	Amyloid beta A4 protein-binding family B member 1	protein	30	0% helix, 50% strand	O00213
B, G	Amyloid beta A4 protein-binding family B member 1	protein	31	0% helix, 48% strand	O00213
D	Amyloid beta A4 protein-binding family B member 1	protein	34	0% helix, 44% strand	O00213
H	Amyloid beta A4 protein-binding family B member 1	protein	33	0% helix, 45% strand	O00213

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, D
PG4 · Tetraethylene glycol · additive · 7 copies · chains A, B, E, C, F, D, H, G

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.31	0.74	17	PG4

Interfaces

12 interfaces between chains.

C–D · 487 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 456 Å² buried · 7 hydrogen bonds · protein-protein
C–F · 303 Å² buried · 5 hydrogen bonds · protein-protein
G–H · 303 Å² buried · 6 hydrogen bonds · protein-protein
E–G · 296 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2IDH · Crystal Structure of human FE65 WW domain · the same entry in another collection · chain H against H, TM-score 1.00
O00213 · AlphaFold monomer V2.0 prediction for amyloid-beta A4 precursor protein-binding family B… · a predicted model of the same protein · chain F against A, TM-score 0.87

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 O00213
Elsewhere: RCSB PDB 2IDH · PDBe 2IDH · UniProt O00213

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