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Crystal structure of plasmodium falciparum ubiquitin carboxyl-terminal hydrolase 3 (UCHL3)

Analyse Crystal structure of plasmodium falciparum ubiquitin carboxyl-terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WE6
Type: protein
Length: 415 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin carboxyl-terminal hydrolase L3
EC: 3.4.19.12
Pockets: 8 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin carboxyl-terminal hydrolase L3 (EC 3.4.19.12)	protein	208	34% helix, 20% strand	—
B	Ubiquitin carboxyl-terminal hydrolase L3 (EC 3.4.19.12)	protein	207	34% helix, 19% strand	—

Pockets

8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	227	0.50	0.75	25	empty
2	153	0.44	0.76	27	empty
3	68	0.36	0.77	14	empty
4	67	0.36	0.77	12	empty
5	79	0.32	0.74	24	empty

Interfaces

1 interface between chains.

A–B · 297 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2WE6 · Crystal Structure of Plasmodium falciparum Ubiquitin Carboxyl- terminal Hydrolase 3… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 2WE6 · PDBe 2WE6

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