MolNFT v1 · #85683 · protein

Von hippel-lindau protein-elonginb-elonginc complex, bound to HIF1- alpha peptide

4AJY: “Von hippel-lindau protein-elonginb-elonginc complex, bound to HIF1- alpha peptide”. X-ray diffraction. MolNFT v1 #85683 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4AJY
Type: protein
Length: 356 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q15370, Q15369, Q16665, P40337

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	—	protein	105	—	Q15370
C	—	protein	88	—	Q15369
H	—	protein	15	—	Q16665
V	—	protein	148	—	P40337

Compared structures

4AJY · von Hippel-Lindau protein-ElonginB-ElonginC complex, bound to Hif1- alpha peptide · the same entry in another collection · chain B against B, TM-score 1.00
Q15370 · AlphaFold monomer V2.0 prediction for elongin-B (Q15370) · a predicted model of the same protein · chain B against A, TM-score 0.97
Q15369 · AlphaFold monomer V2.0 prediction for elongin-C (Q15369) · a predicted model of the same protein · chain C against A, TM-score 0.96
Q16665 · AlphaFold monomer V2.0 prediction for hypoxia-inducible factor 1-alpha (Q16665) · a predicted model of the same protein · chain H against A, TM-score 0.29

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 Q15370
Every structure of UniProt Q15369
Every structure of UniProt Q16665
Every structure of UniProt P40337
Elsewhere: RCSB PDB 4AJY · PDBe 4AJY · UniProt Q15370 · UniProt Q15369 · UniProt Q16665 · UniProt P40337

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