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Mthk rck domain D184N mutant, CA2+-bound

Analyse Mthk rck domain D184N mutant, CA2+-bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RBX
Type: protein
Length: 1,320 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calcium-gated potassium channel mthk
UniProt: O27564
Ligands: CA
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Calcium-gated potassium channel mthk	protein	221	40% helix, 22% strand	O27564
C, E	Calcium-gated potassium channel mthk	protein	220	40% helix, 23% strand	O27564
D, F	Calcium-gated potassium channel mthk	protein	219	39% helix, 23% strand	O27564

Ligands and binding sites

CA · Calcium ion · metal · 12 copies · chains A, B, C, D, E, F

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

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	868	0.79	0.81	55	empty
2	1080	0.78	0.80	71	empty
3	816	0.78	0.81	84	CA
4	277	0.74	0.87	41	CA
5	263	0.70	0.85	36	CA

Interfaces

11 interfaces between chains.

A–B · 3700 Å² buried · 43 hydrogen bonds · protein-protein
E–F · 3659 Å² buried · 40 hydrogen bonds · protein-protein
C–D · 3647 Å² buried · 45 hydrogen bonds · protein-protein
A–D · 713 Å² buried · 0 hydrogen bonds · protein-protein
B–E · 654 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3RBX · MthK RCK domain D184N mutant, Ca2+-bound · the same entry in another collection · chain F against F, TM-score 1.00
O27564 · AlphaFold monomer V2.0 prediction for calcium-gated potassium channel mthk (O27564) · a predicted model of the same protein · chain C against A, TM-score 0.98

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 O27564
Elsewhere: RCSB PDB 3RBX · PDBe 3RBX · UniProt O27564

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