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Crystal structure of apo-PAS1

Analyse Crystal structure of apo-PAS1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HWT
Type: protein
Length: 247 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sensor histidine kinase tods
EC: 2.7.13.3
UniProt: A5W4E3
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sensor histidine kinase tods (EC 2.7.13.3)	protein	125	38% helix, 37% strand	A5W4E3
B	Sensor histidine kinase tods (EC 2.7.13.3)	protein	122	26% helix, 38% strand	A5W4E3

Pockets

5 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	56	0.74	0.99	15	empty
2	50	0.73	0.99	15	empty
3	107	0.59	0.85	20	empty
4	109	0.44	0.78	25	empty
5	128	0.43	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 873 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

5HWT · Crystal structure of apo-PAS1 · the same entry in another collection · chain A against A, TM-score 1.00
A5W4E3 · AlphaFold monomer V2.0 prediction for sensor histidine kinase tods (A5W4E3) · a predicted model of the same protein · chain A against A, TM-score 0.95

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A5W4E3
Elsewhere: RCSB PDB 5HWT · PDBe 5HWT · UniProt A5W4E3

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