Structure of PDB 1y4s Chain B Binding Site BS01

Receptor Information
>1y4s Chain B (length=475) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKGQETRGFQSEVKQLLHLMIHSLYSNKEIFLRELISNASDAADKLRFRA
LSNPDLYEGDGELRVRVSFDKDKRTLTISDNGVGMTRDEVIDHLGTIAKS
GTKSFLESSQLIGQFGVGFYSAFIVADKVTVRTRAAGEKPENGVFWESAG
EGEYTVADITKEDRGTEITLHLREGEDEFLDDWRVRSIISKYSDHIALPV
EIEKREEKDGETVISWEKINKAQALWTRNKSEITDEEYKEFYKHIAHDFN
DPLTWSHNRVEGKQEYTSLLYIPSQAPWDMWNRDHKHGLKLYVQRVFIMD
DAEQFMPNYLRFVRGLIDSSDLPLNVSREILQDSTVTRNLRNALTKRVLQ
MLEKLAKDDAEKYQTFWQQFGLVLKEGPAEDFANQEAIAKLLRFASTHTD
SSAQTVSLEDYVSRMKEGQEKIYYITADSYAAAKSSPHLELLRKKGIEVL
LLSDRIDEWMMNYLTEFDGKPFQSV
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1y4s Chain B Residue 704 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1y4s Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		N38 H255
Binding residue
(residue number reindexed from 1)		N38 H247
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0044183 protein folding chaperone
GO:0051082 unfolded protein binding
GO:0051087 protein-folding chaperone binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0006974 DNA damage response
GO:0009408 response to heat
GO:0043093 FtsZ-dependent cytokinesis
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1y4s, PDBe:1y4s, PDBj:1y4s
PDBsum1y4s
PubMed15837196
UniProtP0A6Z3|HTPG_ECOLI Chaperone protein HtpG (Gene Name=htpG)

[Back to BioLiP]