MolNFT v1 · #79791 · protein

N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: structure of a human CUL1WHB- DCN1P-acetylated UBC12N complex

3TDU: “N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: structure…”. X-ray diffraction. MolNFT v1 #79791 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3TDU
Type: protein
Length: 568 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q96GG9, Q13616, P61081

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	193	—	Q96GG9
B	—	protein	194	—	Q96GG9
C	—	protein	75	—	Q13616
D	—	protein	76	—	Q13616
E, F	—	protein	15	—	P61081

Compared structures

3TDU · N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein… · the same entry in another collection · chain F against F, TM-score 1.00
Q13616 · AlphaFold monomer V2.0 prediction for cullin-1 (Q13616) · a predicted model of the same protein · chain C against A, TM-score 0.98
Q96GG9 · AlphaFold monomer V2.0 prediction for DCN1-like protein 1 (Q96GG9) · a predicted model of the same protein · chain A against A, TM-score 0.98
P61081 · AlphaFold monomer V2.0 prediction for NEDD8-conjugating enzyme UBC12 (P61081) · a predicted model of the same protein · chain E against A, TM-score 0.67

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 Q96GG9
Every structure of UniProt Q13616
Every structure of UniProt P61081
Elsewhere: RCSB PDB 3TDU · PDBe 3TDU · UniProt Q96GG9 · UniProt Q13616 · UniProt P61081

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