MolNFT v1 · #150206 · protein

PVHL:ELOB:ELOC in complex with (4-(1H-pyrrol-1-YL)PHENYL)METHANOL

6GMR: “PVHL:ELOB:ELOC in complex with (4-(1H-pyrrol-1-YL)PHENYL)METHANOL”. X-ray diffraction, 2 ligands (F4K, SO4). MolNFT v1 #150206 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6GMR
Type: protein
Length: 359 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q15370, Q15369, P40337
Ligands: F4K, SO4

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	—	protein	105	—	Q15370
C	—	protein	89	—	Q15369
H	—	protein	16	—	—
V	—	protein	149	—	P40337

Ligands and binding sites

F4K · (4-pyrrol-1-ylphenyl)methanol · ligand · chains V
SO4 · Sulfate ion · ion · chains B, C
GOL · Glycerol · additive · chains C, V

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

Compared structures

6GMR · pVHL:EloB:EloC in complex with (4-(1H-pyrrol-1-yl)phenyl)methanol · 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 0.99
Q15369 · AlphaFold monomer V2.0 prediction for elongin-C (Q15369) · a predicted model of the same protein · chain C against A, TM-score 0.95

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 P40337
Elsewhere: RCSB PDB 6GMR · PDBe 6GMR · UniProt Q15370 · UniProt Q15369 · UniProt P40337

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