MolNFT v2 · #151151 · protein

pVHL:EloB:EloC in complex with 6-chlorothiochroman-4-one

6GMX: “pVHL:EloB:EloC in complex with 6-chlorothiochroman-4-one”. X-ray diffraction at 2.533, 1 ligand (F7B). MolNFT v2 #151151 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6GMX
Type: protein
Length: 1,318 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.533
Source: Homo sapiens
UniProt: Q15370, Q15369, P40337
Ligands: F7B

Structure

x-ray diffraction · resolution 2.533 · 8 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, G, J	—	protein	103	—	Q15370
B, E	—	protein	87	—	Q15369
C	—	protein	138	—	P40337
D	—	protein	96	—	Q15370
F	—	protein	142	—	P40337
H	—	protein	85	—	Q15369
I, L	—	protein	144	—	P40337
K	—	protein	86	—	Q15369

Ligands and binding sites

F7B · 6-chloranyl-2,3-dihydrothiochromen-4-one · ligand · 2 copies · chains B, K
IPA · Isopropyl alcohol · additive · 4 copies · chains C, F, I, L
ACT · Acetate ion · additive · 2 copies · chains E, F, K, L

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

Compared structures

6GMX · PVHL:ELOB:ELOC in complex with 6-chlorothiochroman-4-one · the same entry in another collection · chain L against L, 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 Q15370
Every structure of UniProt Q15369
Every structure of UniProt P40337
Elsewhere: RCSB PDB 6GMX · PDBe 6GMX · UniProt Q15370 · UniProt Q15369 · UniProt P40337

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