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Crystal structure of S. cerevisiae UBC3 (CDC34)

Analyse Crystal structure of S. cerevisiae UBC3 (CDC34) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NYD
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin-conjugating enzyme E2-34 kda
EC: 2.3.2.23
UniProt: P14682
Ligands: ZN
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Ubiquitin-conjugating enzyme E2-34 kda (EC 2.3.2.23)	protein	166	36% helix, 17% strand	P14682

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains C
ACT · Acetate ion · additive · 3 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.30	0.75	14	empty

Compared structures

6NYD · Crystal Structure of S. cerevisiae Ubc3 (Cdc34) · the same entry in another collection · chain C against C, TM-score 1.00
P14682 · AlphaFold monomer V2.0 prediction for ubiquitin-conjugating enzyme E2-34 kda (P14682) · a predicted model of the same protein · chain C 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 P14682
Elsewhere: RCSB PDB 6NYD · PDBe 6NYD · UniProt P14682

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