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Crystal structure of chaperone ESPG3 of esx-3 type VII secretion system from mycobacterium marinum M

Analyse Crystal structure of chaperone ESPG3 of esx-3 type VII secretion system from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DLB
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone ESPG3
UniProt: B2HNX0
Ligands: PT, SCN, SO4
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone ESPG3	protein	263	36% helix, 28% strand	B2HNX0

Ligands and binding sites

PT · Platinum (II) ion · metal · 7 copies · chains A
SCN · Thiocyanate ion · ion · 32 copies · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 3 copies · chains A
CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	268	0.56	0.77	30	CXS, GOL, PT, SCN

Compared structures

5DLB · Crystal structure of chaperone EspG3 of ESX-3 type VII secretion system from… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt B2HNX0
Elsewhere: RCSB PDB 5DLB · PDBe 5DLB · UniProt B2HNX0

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