BioLiP

Receptor Information

>4as9 Chain A (length=213) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLS
DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGT
KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESN
AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV
AYPIQLVVTKEVE

Ligand ID

4QS

InChI

InChI=1S/C30H42N2O9/c1-15-12-20-26(35)23(19(5)25(34)28(20)40-8)32-29(36)16(2)10-9-11-21(38-6)27(41-30(31)37)18(4)14-17(3)24(33)22(13-15)39-7/h9-11,14-15,17,21-22,24,27,33H,12-13H2,1-8H3,(H2,31,37)(H,32,36)/b11-9+,16-10?,18-14+/t15-,17-,21+,22+,24-,27-/m1/s1

InChIKey

CWRDTPRXLNGSCO-ZFBKRPMSSA-N

SMILES

Software	SMILES
ACDLabs 12.01	O=C1C(OC)=C2C(=O)C(=C1C)NC(=O)C(=CC=CC(OC)C(OC(=O)N)C(=CC(C)C(O)C(OC)CC(C)C2)C)C
CACTVS 3.385	CO[CH]1C[CH](C)CC2=C(OC)C(=O)C(=C(NC(=O)C(=CC=C[CH](OC)[CH](OC(N)=O)C(=C[CH](C)[CH]1O)C)C)C2=O)C
OpenEye OEToolkits 1.9.2	CC1CC(C(C(C=C(C(C(C=CC=C(C(=O)NC2=C(C(=O)C(=C(C1)C2=O)OC)C)C)OC)OC(=O)N)C)C)O)OC
OpenEye OEToolkits 1.9.2	C[C@H]1C[C@@H]([C@@H]([C@@H](C=C([C@H]([C@H](/C=C/C=C(C(=O)NC2=C(C(=O)C(=C(C1)C2=O)OC)C)C)OC)OC(=O)N)C)C)O)OC
CACTVS 3.385	CO[C@H]1C[C@H](C)CC2=C(OC)C(=O)C(=C(NC(=O)C(=C/C=C/[C@H](OC)[C@H](OC(N)=O)C(=C/[C@@H](C)[C@H]1O)/C)\C)C2=O)C

Formula

C30 H42 N2 O9

Name

[(3R,5S,6R,7R,10R,11S,12E)-5,11,21-trimethoxy-3,7,9,15,19-pentamethyl-6-oxidanyl-16,20,22-tris(oxidanylidene)-17-azabicyclo[16.3.1]docosa-1(21),8,12,14,18-pentaen-10-yl] carbamate

ChEMBL

DrugBank

ZINC

PDB chain

4as9 Chain A Residue 1215 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	4as9 Synthesis of 19-substituted geldanamycins with altered conformations and their binding to heat shock protein Hsp90.
Resolution	2.71 Å
Binding residue (original residue number in PDB)	N37 A41 K44 M84 E88 N92 K98 G121 V122 F124 T171 V213 E214
Binding residue (residue number reindexed from 1)	N36 A40 K43 M83 E87 N91 K97 G120 V121 F123 T170 V212 E213
Annotation score	1
Binding affinity	PDBbind-CN: -logKd/Ki=4.79,Kd=16.3uM

Enzyme Commision number

	Molecular Function
GO:0005524	ATP binding
GO:0016887	ATP hydrolysis activity
GO:0051082	unfolded protein binding
GO:0140662	ATP-dependent protein folding chaperone

	Biological Process
GO:0006457	protein folding

PDB	RCSB:4as9, PDBe:4as9, PDBj:4as9
PDBsum	4as9
PubMed	23511419
UniProt	P02829\|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

[Back to BioLiP]

Structure of PDB 4as9 Chain A Binding Site BS01