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A trimeric form of the KV7.1 a domain tail, L602M/L606M mutant semet

Analyse A trimeric form of the KV7.1 a domain tail, L602M/L606M mutant semet in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HFC
Type: protein
Length: 77 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium voltage-gated channel subfamily kqt member 1
UniProt: P51787

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Potassium voltage-gated channel subfamily kqt member 1	protein	27	74% helix, 0% strand	P51787
B, C	Potassium voltage-gated channel subfamily kqt member 1	protein	25	80% helix, 0% strand	P51787

Interfaces

3 interfaces between chains.

A–C · 601 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 585 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 502 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3HFC · A trimeric form of the Kv7.1 A domain Tail, L602M/L606M mutant Semet · the same entry in another collection · chain A against A, TM-score 1.00
P51787 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily kqt… · a predicted model of the same protein · chain B against A, TM-score 0.73

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 P51787
Elsewhere: RCSB PDB 3HFC · PDBe 3HFC · UniProt P51787

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