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Structure of ESPG3 chaperone from the type VII (esx-3) secretion system, space group P43212

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

PDB: 4RCL
Type: protein
Length: 492 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ESPG3
UniProt: A0QQ45
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ESPG3	protein	257	32% helix, 32% strand	A0QQ45
B	ESPG3	protein	235	27% helix, 33% strand	A0QQ45

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	1185	0.81	0.82	117	empty
2	55	0.31	0.76	12	empty

Interfaces

1 interface between chains.

A–B · 981 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

4RCL · Structure of EspG3 chaperone from the type VII (ESX-3) secretion system, space group… · the same entry in another collection · chain A against A, TM-score 1.00
A0QQ45 · AlphaFold monomer V2.0 prediction for esx-3 secretion-associated protein ESPG3 (A0QQ45) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 A0QQ45
Elsewhere: RCSB PDB 4RCL · PDBe 4RCL · UniProt A0QQ45

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