Structure of PDB 1atr Chain A

Receptor sequence
>1atrA (length=383) Species: 9913 (Bos taurus) [Search protein sequence]
SKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLI
GDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRP
KVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFN
DSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLG
GGVFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKK
DISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRAR
FEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQ
DFFNGKELNKSINPDEAVAYGAAVQAAILSGDK
3D structure
PDB1atr Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis.
ChainA
Resolution2.34 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) D9 K70 E174 D198
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 PO4 A G12 T13 K71 G11 T12 K70
BS02 ADP A G12 T14 Y15 G201 G202 E268 K271 R272 S275 G339 G11 T13 Y14 G200 G201 E267 K270 R271 S274 G338 PDBbind-CN: -logKd/Ki=6.96,Kd=110nM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:1atr, PDBe:1atr, PDBj:1atr
PDBsum1atr
PubMed8226982
UniProtP19120|HSP7C_BOVIN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

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