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Potassium channel kcsa-Fab complex in cs+

Analyse Potassium channel kcsa-Fab complex in cs+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1R3L
Type: protein
Length: 534 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antibody Fab fragment light chain; Antibody Fab fragment heavy chain; Voltage-gated…
UniProt: P0A334
Ligands: F09, DGA, CS
Pockets: 6 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 18% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Antibody Fab fragment light chain	protein	212	6% helix, 50% strand	—
B	Antibody Fab fragment heavy chain	protein	219	3% helix, 50% strand	—
C	Voltage-gated potassium channel	protein	103	74% helix, 0% strand	P0A334

Ligands and binding sites

F09 · Nonan-1-ol · ligand · chains B, C
DGA · Diacyl glycerol · ligand · chains C
CS · Cesium ion · metal · 5 copies · chains C

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	754	0.68	0.76	59	empty
2	55	0.51	0.88	19	empty
3	223	0.51	0.76	40	empty
4	77	0.50	0.84	18	empty
5	59	0.50	0.85	14	empty

Interfaces

3 interfaces between chains.

A–B · 1751 Å² buried · 17 hydrogen bonds · protein-protein
B–C · 475 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 438 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1R3L · potassium channel KcsA-Fab complex in Cs+ · the same entry in another collection · chain A against A, TM-score 1.00
P0A334 · AlphaFold monomer V2.0 prediction for pH-gated potassium channel kcsa (P0A334) · a predicted model of the same protein · chain C against A, TM-score 0.97

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 P0A334
Elsewhere: RCSB PDB 1R3L · PDBe 1R3L · UniProt P0A334

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