MolNFT v1 · #85970 · protein

The structure of modified benzoquinone ansamycins bound to yeast N- terminal HSP90

4ASF · ATP-dependent molecular chaperone HSP82: “The structure of modified benzoquinone ansamycins bound to yeast N- terminal HSP90”. X-ray diffraction, 2 ligands (62U, NI), 1 pocket (best druggability 0.59). MolNFT v1 #85970 on GenesisL1…

PDB: 4ASF
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent molecular chaperone HSP82
UniProt: P02829
Ligands: 62U, NI
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent molecular chaperone HSP82	protein	213	42% helix, 22% strand	P02829

Ligands and binding sites

62U · (8S,9R,13R,14S,16R)-21-(furan-2-yl)-13-hydroxy-8,14,19-trimethoxy-16-methyl-4,10,12-trimethylidene-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),18-dien-9-yl carbamate · ligand · chains A
NI · Nickel (II) ion · metal · 3 copies · 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	228	0.59	0.80	27	62U

Compared structures

4ASF · The structure of modified benzoqui ansamycins bound to yeast N- terminal Hsp90 · the same entry in another collection · chain A against A, 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 P02829
Elsewhere: RCSB PDB 4ASF · PDBe 4ASF · UniProt P02829

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