MolNFT v1 · #167816 · protein

C-terminal regulatory domain of the chloride transporter kcc-1 from C. elegans

6VWA · K+/CL-cotransporter: “C-terminal regulatory domain of the chloride transporter kcc-1 from C. elegans”. X-ray diffraction, 3 pockets (best druggability 0.68). MolNFT v1 #167816 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6VWA
Type: protein
Length: 325 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: K+/CL-cotransporter
UniProt: S6FCX2
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	K+/CL-cotransporter	protein	325	49% helix, 19% strand	S6FCX2

Ligands and binding sites

PGE · Triethylene glycol · additive · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	397	0.68	0.80	54	PEG
2	188	0.49	0.76	23	PEG
3	148	0.45	0.75	24	PGE

Compared structures

6VWA · C-terminal regulatory domain of the chloride transporter KCC-1 from C. elegans · 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 S6FCX2
Elsewhere: RCSB PDB 6VWA · PDBe 6VWA · UniProt S6FCX2

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