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Sarr mbp fusion structure

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

PDB: 1HSJ
Type: protein
Length: 974 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fusion protein consisting of staphylococcus accessory regulator protein R and maltose…
UniProt: P0AEY0, Q2YYV0
Ligands: GLC
Pockets: 13 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fusion protein consisting of staphylococcus accessory regulator protein R and maltose binding protein	protein	487	47% helix, 16% strand	P0AEY0, Q2YYV0

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	497	0.78	0.85	50	empty
2	273	0.74	0.87	29	GLC
3	328	0.72	0.84	29	GLC
4	379	0.68	0.81	38	empty
5	466	0.66	0.78	42	empty

Interfaces

1 interface between chains.

A–B · 2140 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

1HSJ · Sarr mbp fusion structure · the same entry in another collection · chain A against A, TM-score 1.00
Q2YYV0 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator sarr (Q2YYV0) · a predicted model of the same protein · chain A against A, TM-score 0.23

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 P0AEY0
Every structure of UniProt Q2YYV0
Elsewhere: RCSB PDB 1HSJ · PDBe 1HSJ · UniProt P0AEY0 · UniProt Q2YYV0

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