Structure of PDB 1hpm Chain A Binding Site BS01

Receptor Information

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

GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGD
AAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKV
QVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDS
QRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGG
TFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDI
SENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFE
ELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDF
FNGKELNKSINPDEAVAYGAAVQAAILS

Ligand information

• Ligand ID: PO4
• InChI: InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
• InChIKey: NBIIXXVUZAFLBC-UHFFFAOYSA-K
• SMILES:
  CACTVS 3.341: [O-][P]([O-])([O-])=O
  ACDLabs 10.04: [O-]P([O-])([O-])=O
  OpenEye OEToolkits 1.5.0: [O-]P(=O)([O-])[O-]
• Formula: O4 P
• Name: PHOSPHATE ION
• DrugBank: DB14523
• PDB chain: 1hpm Chain A Residue 488

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): G12 T13 K71 E175 T204
• Binding residue (residue number reindexed from 1): G9 T10 K68 E172 T201
• 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)