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Heag pas domain

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

PDB: 5J7E
Type: protein
Length: 646 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium voltage-gated channel subfamily H member 1
UniProt: O95259
Pockets: 6 · best druggability 0.54

Structure

x-ray diffraction · 5 distinct chains · 24% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Potassium voltage-gated channel subfamily H member 1	protein	109	23% helix, 39% strand	O95259
B, E	Potassium voltage-gated channel subfamily H member 1	protein	108	24% helix, 38% strand	O95259
C	Potassium voltage-gated channel subfamily H member 1	protein	110	24% helix, 38% strand	O95259
D	Potassium voltage-gated channel subfamily H member 1	protein	106	25% helix, 40% strand	O95259
F	Potassium voltage-gated channel subfamily H member 1	protein	105	25% helix, 39% strand	O95259

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	314	0.54	0.75	48	empty
2	206	0.52	0.77	38	empty
3	172	0.52	0.79	33	empty
4	54	0.45	0.84	19	empty
5	66	0.29	0.73	15	empty

Interfaces

8 interfaces between chains.

A–D · 776 Å² buried · 3 hydrogen bonds · protein-protein
C–E · 753 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 469 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 441 Å² buried · 4 hydrogen bonds · protein-protein
A–E · 336 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5J7E · hEAG PAS domain · the same entry in another collection · chain F against F, TM-score 1.00
O95259 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily H member… · a predicted model of the same protein · chain D 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 O95259
Elsewhere: RCSB PDB 5J7E · PDBe 5J7E · UniProt O95259

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