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Structure of ppsr N-Q-PAS1 from rb. sphaeroides

Analyse Structure of ppsr N-Q-PAS1 from rb. sphaeroides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L9G
Type: protein
Length: 496 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional regulator, ppsr
UniProt: Q3J179
Ligands: SO4
Pockets: 5 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional regulator, ppsr	protein	250	38% helix, 31% strand	Q3J179
B	Transcriptional regulator, ppsr	protein	246	38% helix, 30% strand	Q3J179

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.51	0.83	16	empty
2	156	0.50	0.78	23	empty
3	52	0.33	0.78	15	empty
4	58	0.33	0.77	16	empty
5	58	0.32	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 3177 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

4L9G · Structure of PpsR N-Q-PAS1 from Rb. sphaeroides · the same entry in another collection · chain A against A, TM-score 1.00

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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 Q3J179
Elsewhere: RCSB PDB 4L9G · PDBe 4L9G · UniProt Q3J179

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