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Crystal structure of the C-terminal region of human ZFYVE9

Analyse Crystal structure of the C-terminal region of human ZFYVE9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BKW
Type: protein
Length: 479 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Zinc finger fyve domain-containing protein 9
UniProt: O95405
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zinc finger fyve domain-containing protein 9	protein	479	23% helix, 34% strand	O95405

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 5 copies · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	846	0.73	0.78	77	EDO
2	262	0.53	0.76	33	empty
3	71	0.36	0.77	16	empty
4	86	0.36	0.76	15	empty

Compared structures

4BKW · Crystal structure of the C-terminal region of human ZFYVE9 · the same entry in another collection · chain A against A, TM-score 1.00
O95405 · AlphaFold monomer V2.0 prediction for zinc finger fyve domain- containing protein 9… · a predicted model of the same protein · 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 O95405
Elsewhere: RCSB PDB 4BKW · PDBe 4BKW · UniProt O95405

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