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Structure and interactions of pas kinase N-terminal pas domain: model for intramolecular kinase regulation

Analyse Structure and interactions of pas kinase N-terminal pas domain: model for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LL8
Type: protein
Length: 114 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pas kinase
EC: 2.7.1.37
UniProt: Q96RG2
Pockets: 1 · best druggability 0.33

Structure

solution nmr · 1 distinct chain · 12% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pas kinase (EC 2.7.1.37)	protein	114	12% helix, 25% strand	Q96RG2

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.33	0.77	17	empty

Compared structures

1LL8 · Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular… · the same entry in another collection · chain A against A, TM-score 1.00
Q96RG2 · AlphaFold monomer V2.0 prediction for pas domain-containing SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.66

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 Q96RG2
Elsewhere: RCSB PDB 1LL8 · PDBe 1LL8 · UniProt Q96RG2

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