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HUMAN NKCC1

Analyse HUMAN NKCC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D10
Type: protein
Length: 892 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Solute carrier family 12 member 2
UniProt: P55011
Ligands: PLM
Pockets: 11 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 58% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Solute carrier family 12 member 2	protein	446	58% helix, 0% strand	P55011

Ligands and binding sites

PLM · Palmitic acid · ligand · 4 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	832	0.83	0.84	53	PLM
2	392	0.64	0.78	54	empty
3	384	0.63	0.78	50	empty
4	179	0.59	0.82	31	empty
5	206	0.59	0.80	31	empty

Interfaces

1 interface between chains.

A–B · 655 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7D10 · Human NKCC1 · the same entry in another collection · chain A against A, TM-score 1.00
P55011 · AlphaFold monomer V2.0 prediction for solute carrier family 12 member 2 (P55011) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P55011
Elsewhere: RCSB PDB 7D10 · PDBe 7D10 · UniProt P55011

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