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Crystal structure of the lipid scramblase NHTMEM16 in crystal form 1

Analyse Crystal structure of the lipid scramblase NHTMEM16 in crystal form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WIS
Type: protein
Length: 1,308 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipid scramblase
UniProt: C7Z7K1
Ligands: CA
Pockets: 19 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipid scramblase	protein	654	69% helix, 5% strand	C7Z7K1

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B

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

Pockets

19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	766	0.75	0.80	76	empty
2	836	0.73	0.78	101	empty
3	882	0.71	0.76	69	empty
4	702	0.70	0.77	61	empty
5	612	0.66	0.76	47	empty

Interfaces

1 interface between chains.

A–B · 4801 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4WIS · Crystal structure of the lipid scramblase nhTMEM16 in crystal form 1 · 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 C7Z7K1
Elsewhere: RCSB PDB 4WIS · PDBe 4WIS · UniProt C7Z7K1

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