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Crystal structure of ubiquitin conjugating enzyme E2 UBCA1 from agrocybe aegerita

Analyse Crystal structure of ubiquitin conjugating enzyme E2 UBCA1 from agrocybe… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WE5
Type: protein
Length: 282 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin conjugating enzyme
EC: 6.3.2.19
UniProt: H9CTH3
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ubiquitin conjugating enzyme (EC 6.3.2.19)	protein	141	28% helix, 19% strand	H9CTH3

Ligands and binding sites

ACY · Acetic acid · additive · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	88	0.54	0.85	18	empty
2	117	0.41	0.76	20	empty
3	113	0.41	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 562 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3WE5 · Crystal structure of ubiquitin conjugating enzyme E2 UbcA1 from Agrocybe aegerita · 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 H9CTH3
Elsewhere: RCSB PDB 3WE5 · PDBe 3WE5 · UniProt H9CTH3

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