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Structure of chlamydia trachomatis effector protein CHLADUB1

Analyse Structure of chlamydia trachomatis effector protein CHLADUB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HAG
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deubiquitinase and deneddylase DUB1
EC: 3.4.22.-
UniProt: B0B9A0
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deubiquitinase and deneddylase DUB1 (EC 3.4.22.-)	protein	266	45% helix, 10% strand	B0B9A0

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

3 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	157	0.63	0.85	25	GOL
2	89	0.43	0.79	23	empty
3	64	0.33	0.76	13	empty

Compared structures

5HAG · Structure of Chlamydia trachomatis effector protein ChlaDUB1 · the same entry in another collection · chain A against A, TM-score 1.00
B0B9A0 · AlphaFold monomer V2.0 prediction for deubiquitinase and deneddylase DUB1 (B0B9A0) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 B0B9A0
Elsewhere: RCSB PDB 5HAG · PDBe 5HAG · UniProt B0B9A0

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