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Crystal structure of UBL123 with an EZH2 peptide

Analyse Crystal structure of UBL123 with an EZH2 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6P5L
Type: protein
Length: 687 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin carboxyl-terminal hydrolase 7; Pro-arg-lys-lys-lys-arg-lys-his
EC: 3.4.19.12
UniProt: Q93009
Pockets: 7 · best druggability 0.48

Structure

x-ray diffraction · 3 distinct chains · 24% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12)	protein	341	23% helix, 32% strand	Q93009
B	Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12)	protein	340	25% helix, 29% strand	Q93009
D	Pro-arg-lys-lys-lys-arg-lys-his	protein	6	0% helix, 0% strand	—

Pockets

7 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	218	0.48	0.74	30	empty
2	148	0.39	0.73	19	empty
3	82	0.38	0.77	18	empty
4	58	0.34	0.77	11	empty
5	60	0.33	0.77	12	empty

Interfaces

2 interfaces between chains.

A–B · 839 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 529 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6P5L · Crystal Structure of Ubl123 with an EZH2 peptide · the same entry in another collection · chain A against A, TM-score 1.00

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 Q93009
Elsewhere: RCSB PDB 6P5L · PDBe 6P5L · UniProt Q93009

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