Structure of PDB 1y4s Chain A

Receptor sequence
>1y4sA (length=475) Species: 562 (Escherichia coli) [Search protein sequence]
MKGQETRGFQSEVKQLLHLMIHSLYSNKEIFLRELISNASDAADKLRFRA
LSNPDLYEGDGELRVRVSFDKDKRTLTISDNGVGMTRDEVIDHLGTIAKS
GTKSFLESSQLIGQFGVGFYSAFIVADKVTVRTRAAGEKPENGVFWESAG
EGEYTVADITKEDRGTEITLHLREGEDEFLDDWRVRSIISKYSDHIALPV
EIEKREEKDGETVISWEKINKAQALWTRNKSEITDEEYKEFYKHIAHDFN
DPLTWSHNRVEGKQEYTSLLYIPSQAPWDMWNRDHKHGLKLYVQRVFIMD
DAEQFMPNYLRFVRGLIDSSDLPLNVSREILQDSTVTRNLRNALTKRVLQ
MLEKLAKDDAEKYQTFWQQFGLVLKEGPAEDFANQEAIAKLLRFASTHTD
SSAQTVSLEDYVSRMKEGQEKIYYITADSYAAAKSSPHLELLRKKGIEVL
LLSDRIDEWMMNYLTEFDGKPFQSV
3D structure
PDB1y4s Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding.
ChainA
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP A N38 M85 H93 G126 F127 T174 H255 N38 M85 H93 G118 F119 T166 H247
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

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

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