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Crystal structure of the sinorhizobium meliloti ai-2 receptor, smlsrb

Analyse Crystal structure of the sinorhizobium meliloti ai-2 receptor, smlsrb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EJW
Type: protein
Length: 630 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Smlsrb
UniProt: Q926H7
Ligands: PAV
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Smlsrb	protein	315	43% helix, 21% strand	Q926H7

Ligands and binding sites

PAV · (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	975	0.77	0.79	95	empty
2	89	0.37	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 727 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3EJW · Crystal Structure of the Sinorhizobium meliloti AI-2 receptor, SmLsrB · the same entry in another collection · chain A against A, TM-score 1.00

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 Q926H7
Elsewhere: RCSB PDB 3EJW · PDBe 3EJW · UniProt Q926H7

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