Structure of PDB 4h5t Chain A

Receptor sequence
>4h5tA (length=382) Species: 9606 (Homo sapiens) [Search protein sequence]
KGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIG
DAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPK
VQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFND
SQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGG
GTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKD
ISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARF
EELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQD
FFNGKELNKSINPDEAVAYGAAVQAAILSGDK
3D structure
PDB4h5t New crystal structures of HSC-70 ATP binding domain confirm the role of individual binding pockets and suggest a new method of inhibition.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D10 K71 E175 D199
Catalytic site (residue number reindexed from 1) D8 K69 E173 D197
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
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 T13 T14 Y15 G201 G202 E268 K271 R272 S275 G339 R342 D366 T11 T12 Y13 G199 G200 E266 K269 R270 S273 G337 R340 D364
BS02 PO4 A G12 T13 K71 E175 T204 G10 T11 K69 E173 T202
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:4h5t, PDBe:4h5t, PDBj:4h5t
PDBsum4h5t
PubMed25433210
UniProtP11142|HSP7C_HUMAN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

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