MolNFT v1 · #101110 · protein

Correlation between chemotype-dependent binding conformations of HSP90 ALPHA/BETA and isoform selectivity

4NH9 · Endoplasmin: “Correlation between chemotype-dependent binding conformations of HSP90 ALPHA/BETA and isoform selectivity”. X-ray diffraction, 1 ligand (2LC), 1 pocket (best druggability 0.61). MolNFT v1 #101110 on GenesisL1: 3D…

PDB: 4NH9
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoplasmin
UniProt: P14625
Ligands: 2LC
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoplasmin	protein	214	36% helix, 24% strand	P14625

Ligands and binding sites

2LC · 2-fluoro-6-[(3S)-tetrahydrofuran-3-ylamino]-4-(3,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indol-1-yl)benzamide · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	235	0.61	0.80	25	2LC

Compared structures

4NH9 · Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and… · the same entry in another collection · chain A against A, TM-score 1.00
P14625 · AlphaFold monomer V2.0 prediction for endoplasmin (P14625) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 P14625
Elsewhere: RCSB PDB 4NH9 · PDBe 4NH9 · UniProt P14625

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