Structure of PDB 7krv Chain A

Receptor sequence
>7krvA (length=538) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
GKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVG
QPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDA
WVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQR
QATKDAGRIAGLEVKCIINEPTAAALAYGLDKGTGNRTIAVYDLGGGAFD
ISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGID
LRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVT
RAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQK
KVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGI
ETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADN
KSLGQFNLDGINPAPRGMPQIEVTFDIDCDGILHVSAKDKNSGKEQKITI
KASSGLNEDEIQKMVRDAEANAEADRKFEELVRLLLTG
3D structure
PDB7krv Conformational equilibria in allosteric control of Hsp70 chaperones.
ChainA
Resolution1.92 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 ATP A G10 T11 T12 N13 K70 G197 G198 G229 E267 K270 I271 S274 G341 G342 Q343 R345 G9 T10 T11 N12 K69 G196 G197 G228 E266 K269 I270 S273 G340 G341 Q342 R344
BS02 6LN A C167 C480 C166 C479
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:7krv, PDBe:7krv, PDBj:7krv
PDBsum7krv
PubMed34453889
UniProtP0A6Y8|DNAK_ECOLI Chaperone protein DnaK (Gene Name=dnaK)

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