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Crystal structure of the uba domain from human C-cbl ubiquitin ligase

Analyse Crystal structure of the uba domain from human C-cbl ubiquitin ligase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OO9
Type: protein
Length: 131 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase cbl
EC: 6.3.2.-
UniProt: P22681

Structure

x-ray diffraction · 3 distinct chains · 72% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase cbl (EC 6.3.2.-)	protein	46	70% helix, 4% strand	P22681
B	E3 ubiquitin-protein ligase cbl (EC 6.3.2.-)	protein	44	75% helix, 0% strand	P22681
C	E3 ubiquitin-protein ligase cbl (EC 6.3.2.-)	protein	41	71% helix, 0% strand	P22681

Interfaces

3 interfaces between chains.

A–B · 580 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 299 Å² buried · 1 hydrogen bond · protein-protein
B–C · 228 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

2OO9 · crystal structure of the UBA domain from human c-Cbl ubiquitin ligase · the same entry in another collection · chain A against A, TM-score 1.00
P22681 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase cbl (P22681) · a predicted model of the same protein · chain C against A, TM-score 0.92

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 P22681
Elsewhere: RCSB PDB 2OO9 · PDBe 2OO9 · UniProt P22681

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