Structure of PDB 1ngj Chain A

Receptor sequence
>1ngjA (length=382) Species: 9913 (Bos taurus) [Search protein sequence]
KGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIG
DAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPK
VQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFND
SQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGG
GTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKD
ISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARF
EELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQD
FFNGKELNKSINPDEAVAYGAAVQAAILSGDK
3D structure
PDB1ngj 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
Resolution2.1 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 ANP A G12 T13 T14 Y15 G201 G202 G203 T204 G230 E268 K271 R272 S275 G338 G339 R342 G10 T11 T12 Y13 G199 G200 G201 T202 G228 E266 K269 R270 S273 G336 G337 R340
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:1ngj, PDBe:1ngj, PDBj:1ngj
PDBsum1ngj
PubMed8175707
UniProtP19120|HSP7C_BOVIN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

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