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Structure of the deamidase-depupylase dop of the prokaryotic ubiquitin-like modification pathway

Analyse Structure of the deamidase-depupylase dop of the prokaryotic ubiquitin-like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4B0R
Type: protein
Length: 456 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deamidase-depupylase dop
EC: 3.4.-.-, 3.5.1.-
UniProt: A0LU48
Pockets: 7 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deamidase-depupylase dop (EC 3.4.-.-, 3.5.1.-)	protein	456	44% helix, 17% strand	A0LU48

Pockets

7 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	83	0.74	0.97	21	empty
2	127	0.48	0.79	21	empty
3	114	0.43	0.77	25	empty
4	81	0.36	0.76	12	empty
5	66	0.36	0.77	20	empty

Compared structures

4B0R · Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification… · the same entry in another collection · chain A against A, TM-score 1.00
A0LU48 · AlphaFold monomer V2.0 prediction for depupylase (A0LU48) · 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 A0LU48
Elsewhere: RCSB PDB 4B0R · PDBe 4B0R · UniProt A0LU48

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