Structure of PDB 2v7y Chain A

Receptor sequence
>2v7yA (length=504) Species: 235909 (Geobacillus kaustophilus HTA426) [Search protein sequence]
MSKIIGIDLGTTNSCVAVLEGGEVKVIPNPEGNRTTPSVVAFKNGERLVG
EVAKRQAITNPNTIISIKRHMGTDYKVEIEGKQYTPQEISAIILQYLKSY
AEDYLGEPVTRAVITVPAYFNDAQRQATKDAGRIAGLEVERIINEPTAAA
LAYGLDKEEDQTILVYDLGGGTFDVSILELGDGVFEVKATAGDNHLGGDD
FDQVIIDYLVNQFKQEHGIDLSKDKMALQRLKDAAEKAKKELSGVTQTQI
SLPFISANENGPLHLEMTLTRAKFEELSAHLVERTMGPVRQALQDAGLTP
ADIDKVILVGGSTRIPAVQEAIKRELGKEPHKGVNPDEVVAIGAAIQGGV
IAGEVKDVVLLDVTPLSLGIETMGGVFTKLIERNTTIPTSKSQVFTTAAD
NQTTVDIHVLQGERPMAADNKSLGRFQLTGIPPAPRGVPQIEVTFDIDAN
GIVHVRAKDLGTNKEQSITIKSSSGLSEEEIQRMIKEAEENAEADRKRKE
AAEL
3D structure
PDB2v7y Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation.
ChainA
Resolution2.37 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 K68 E145 D167
Catalytic site (residue number reindexed from 1) D8 K68 E145 D167
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 T12 N13 G169 G170 G198 E236 K239 K240 S243 G310 G311 S312 R314 T12 N13 G169 G170 G198 E236 K239 K240 S243 G310 G311 S312 R314
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2v7y, PDBe:2v7y, PDBj:2v7y
PDBsum2v7y
PubMed18400763
UniProtQ5KWZ7|DNAK_GEOKA Chaperone protein DnaK (Gene Name=dnaK)

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