Structure of PDB 4b9q Chain C

Receptor sequence
>4b9qC (length=595) Species: 562 (Escherichia coli) [Search protein sequence]
GKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGCTLVG
QPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDA
WVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQR
QATKDAGRIAGLEVKRIINEPTAAALAYGRTIAVYDLGGGAFDISIIEID
EVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLA
MQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESL
VEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFG
KEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVM
TTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFN
LDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLN
EDEIQKMVRDAEANAEADRKCEELVQTRNQGDHLLHSTRKQVEEAGDKLP
ADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQ
3D structure
PDB4b9q Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones
ChainC
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D8 K70 E171 D194
Catalytic site (residue number reindexed from 1) D7 K69 E170 D186
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 ATP C G10 T11 T12 N13 K70 G196 G197 G198 A199 G229 E267 K270 I271 S274 G341 G342 Q343 R345 G9 T10 T11 N12 K69 G188 G189 G190 A191 G221 E259 K262 I263 S266 G333 G334 Q335 R337
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016887 ATP hydrolysis activity
GO:0016989 sigma factor antagonist activity
GO:0031072 heat shock protein binding
GO:0043531 ADP binding
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:0006260 DNA replication
GO:0006457 protein folding
GO:0009408 response to heat
GO:0034620 cellular response to unfolded protein
GO:0042026 protein refolding
GO:0043335 protein unfolding
GO:0045892 negative regulation of DNA-templated transcription
GO:0051085 chaperone cofactor-dependent protein refolding
GO:0065003 protein-containing complex assembly
GO:1990169 stress response to copper ion
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0016234 inclusion body
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4b9q, PDBe:4b9q, PDBj:4b9q
PDBsum4b9q
PubMed23123194
UniProtP0A6Y8|DNAK_ECOLI Chaperone protein DnaK (Gene Name=dnaK)

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