MolNFT v1 · #161687 · protein

Cryo-EM structure of calcium-bound NHTMEM16 lipid scramblase in ddm

6QM5 · Predicted protein: “Cryo-EM structure of calcium-bound NHTMEM16 lipid scramblase in ddm”. Electron microscopy, 1 ligand (CA), 20 pockets (best druggability 0.81). MolNFT v1 #161687 on GenesisL1: 3D structure, binding sites and…

PDB: 6QM5
Type: protein
Length: 1,346 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Predicted protein
UniProt: C7Z7K1
Ligands: CA
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 61% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Predicted protein	protein	673	61% helix, 4% 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

20 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	1078	0.81	0.82	112	empty
2	559	0.74	0.81	61	empty
3	849	0.69	0.75	68	empty
4	800	0.69	0.75	65	empty
5	278	0.61	0.79	37	empty

Interfaces

1 interface between chains.

A–B · 5172 Å² buried · 50 hydrogen bonds · protein-protein

Compared structures

6QM5 · Cryo-EM structure of calcium-bound nhTMEM16 lipid scramblase in DDM · 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 6QM5 · PDBe 6QM5 · UniProt C7Z7K1

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