Structure of PDB 1nge Chain A

Receptor sequence
>1ngeA (length=378) Species: 9913 (Bos taurus) [Search protein sequence]
GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGD
AAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKV
QVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDS
QRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFSLGGG
TFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDI
SENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFE
ELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDF
FNGKELNKSINPDEAVAYGAAVQAAILS
3D structure
PDB1nge Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.
ChainA
Resolution2.05 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 S199
Catalytic site (residue number reindexed from 1) D7 K68 E172 S196
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 ATP A G12 T13 T14 Y15 G201 G202 G203 T204 G230 E268 K271 R272 S275 G338 G339 R342 G9 T10 T11 Y12 G198 G199 G200 T201 G227 E265 K268 R269 S272 G335 G336 R339
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:1nge, PDBe:1nge, PDBj:1nge
PDBsum1nge
PubMed8175707
UniProtP19120|HSP7C_BOVIN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

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