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NMR studies of a channel protein without membrane: structure and dynamics of water-solubilized kcsa

Analyse NMR studies of a channel protein without membrane: structure and dynamics of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KB1
Type: protein
Length: 412 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: WSK3
Pockets: 10 · best druggability 0.84

Structure

solution nmr · 1 distinct chain · 68% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	WSK3	protein	103	68% helix, 0% strand	—

Pockets

10 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	1025	0.84	0.84	74	empty
2	100	0.45	0.79	19	empty
3	105	0.44	0.78	15	empty
4	84	0.39	0.77	13	empty
5	58	0.38	0.79	13	empty

Interfaces

5 interfaces between chains.

A–B · 1007 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 950 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 944 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 839 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 20 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2KB1 · NMR studies of a channel protein without membrane: structure and dynamics of… · 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
Elsewhere: RCSB PDB 2KB1 · PDBe 2KB1

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