Structure of PDB 1hpm Chain A Binding Site BS03

Receptor Information

>1hpm Chain A (length=378) Species: 9913 (Bos taurus)

GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGD
AAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKV
QVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDS
QRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGG
TFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDI
SENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFE
ELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDF
FNGKELNKSINPDEAVAYGAAVQAAILS

Ligand information

• Ligand ID: K
• InChI: InChI=1S/K/q+1
• InChIKey: NPYPAHLBTDXSSS-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [K+]
• Formula: K
• Name: POTASSIUM ION
• ChEMBL: CHEMBL1233793
• DrugBank: DB01345
• PDB chain: 1hpm Chain A Residue 491

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1hpm How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site.
• Resolution: 1.7 Å
• Binding residue (original residue number in PDB): D199 L200 G201 T204 F205 D206
• Binding residue (residue number reindexed from 1): D196 L197 G198 T201 F202 D203
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): D10 K71 E175 D199
• Catalytic site (residue number reindexed from 1): D7 K68 E172 D196
• Enzyme Commision number: 3.6.4.10: non-chaperonin molecular chaperone ATPase.

Gene Ontology

Molecular Function

• GO:0005524 ATP binding
• GO:0140662 ATP-dependent protein folding chaperone

External links

• PDB: RCSB:1hpm, PDBe:1hpm, PDBj:1hpm
• PDBsum: 1hpm
• PubMed: 7836458
• UniProt: P19120|HSP7C_BOVIN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)