Structure of PDB 5tvu Chain A

Receptor sequence
>5tvuA (length=588) Species: 7955 (Danio rerio) [Search protein sequence]
TLHNIITDTENVQGSFSKHEFQAETKKLLDIVARSLYSEKEVFIRELISN
GSDALEKLRHRMITAGGAPMEIHLQTDSVKGTFTIQDTGVGMNKEDLVSN
LGTIARSGSKAFLDALQNQAEASSSIIGQFGVGFYSAFMVADKVEVYSQS
AEAPGYKWSSDGSGVFEVAEASGVRQGTKIVLHLKDDCKEFSSEDRVKEV
VTKYSNFVSFPIFLNGRRLNTLQALWMMEPKDISEWQHEEFYRYVAQAYD
KPRYTLHYRADAPLNIRSIFYVPEMKPSMFDSSVALYSRKILIQTKATDI
LPKWLRFLRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRVIRFLLDQ
SKKDPEKYARFFEDYGLFMREGIVTTGEQSVKEDIAKLLRFESSALPAGQ
QTSLMEYSSRMKAGTRNIYYLCAPNRHLAEHSPYFEAMKQKDMEVLFCFE
QFDELTLLHLREFDRKKLISAERLSSEQAEDLLAWMRNALVQRVTNIKVT
PRLDTHPAMITVLEMGAARHFLRLQPTLEINTGHDLIKKLHALKDSNPEL
AQLLLEQIYDNAMIAAGLNEDPRPMISRLNQLLTRALE
3D structure
PDB5tvu Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.
ChainA
Resolution3.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 N134 A138 M178 N186 S193 G194 S195 G214 Q215 F216 G217 V218 G219 F220 T266 R417 N50 A54 M92 N100 S107 G108 S109 G128 Q129 F130 G131 V132 G133 F134 T178 R323
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005509 calcium ion binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0019901 protein kinase binding
GO:0042802 identical protein binding
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5tvu, PDBe:5tvu, PDBj:5tvu
PDBsum5tvu
PubMed28742020
UniProtF1Q9X9

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