MolNFT v1 · #165014 · protein

Domain swapped E6AP C-lobe dimer

6TGK · Ubiquitin-protein ligase E3A: “Domain swapped E6AP C-lobe dimer”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.56). MolNFT v1 #165014 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6TGK
Type: protein
Length: 105 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin-protein ligase E3A
EC: 2.3.2.26
UniProt: Q05086
Ligands: CA
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Ubiquitin-protein ligase E3A (EC 2.3.2.26)	protein	105	44% helix, 6% strand	Q05086

Ligands and binding sites

CA · Calcium ion · metal · chains C
ACT · Acetate ion · additive · 2 copies · chains C

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	324	0.56	0.75	36	empty

Compared structures

6TGK · Domain swapped E6AP C-lobe dimer · the same entry in another collection · chain C against C, TM-score 1.00
Q05086 · AlphaFold monomer V2.0 prediction for ubiquitin-protein ligase E3A (Q05086) · a predicted model of the same protein · chain C against A, TM-score 0.75

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 Q05086
Elsewhere: RCSB PDB 6TGK · PDBe 6TGK · UniProt Q05086

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