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Crystal structure of a bacterial signalling complex

Analyse Crystal structure of a bacterial signalling complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZHY
Type: protein
Length: 262 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Yfir; Yfib
UniProt: Q9I4L4, Q9I4L6
Ligands: SO4
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Yfir	protein	150	33% helix, 24% strand	Q9I4L4
B	Yfib	protein	112	43% helix, 17% strand	Q9I4L6

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
FMT · Formic acid · additive · 4 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	146	0.57	0.82	23	empty
2	134	0.56	0.82	19	empty

Interfaces

1 interface between chains.

A–B · 1088 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4ZHY · Crystal structure of a bacterial signalling complex · 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 Q9I4L4
Every structure of UniProt Q9I4L6
Elsewhere: RCSB PDB 4ZHY · PDBe 4ZHY · UniProt Q9I4L4 · UniProt Q9I4L6

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