MolNFT v1 · #171826 · protein

Yeast UBA1 in complex with UBC3 and ATP

6ZHU: “Yeast UBA1 in complex with UBC3 and ATP”. X-ray diffraction, 2 ligands (ATP, MG). MolNFT v1 #171826 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6ZHU
Type: protein
Length: 4,681 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P14682, P22515
Ligands: ATP, MG

Structure

x-ray diffraction · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	—	protein	177	—	P14682
F, H	—	protein	178	—	P14682
D	—	protein	173	—	P14682
A, C	—	protein	995	—	P22515
E	—	protein	993	—	P22515
G	—	protein	992	—	P22515

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, E, C, G
MG · Magnesium ion · metal · 4 copies · chains A, E, C, G

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

Compared structures

6ZHU · Yeast Uba1 in complex with Ubc3 and ATP · the same entry in another collection · chain G against G, TM-score 1.00
P22515 · AlphaFold monomer V2.0 prediction for ubiquitin-activating enzyme E1 1 (P22515) · a predicted model of the same protein · chain A against A, TM-score 0.99
P14682 · AlphaFold monomer V2.0 prediction for ubiquitin-conjugating enzyme E2-34 kda (P14682) · a predicted model of the same protein · chain D against A, TM-score 0.91

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
Every structure of UniProt P22515
Elsewhere: RCSB PDB 6ZHU · PDBe 6ZHU · UniProt P14682 · UniProt P22515

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