Structure of PDB 7exp Chain B

Receptor sequence
>7expB (length=599) Species: 7955 (Danio rerio) [Search protein sequence]
TLHNIITDTENVQGSFSKHEFQAETKKLLDIVARSLYSEKEVFIRELISN
GSDALEKLRHRMITTAPMEIHLQTDSVKGTFTIQDTGVGMNKEDLVSNLG
TIARSGSKAFLDSSSIIGQFGVGFYSAFMVADKVEVYSQSAEADAPGYKW
SSDGSGVFEVAEASGVRQGTKIVLHLKDDCKEFSSEDRVKEVVTKYSNFV
SFPIFLNGRRLNTLQALWMMEPKDISEWQHEEFYRYVAQAYDKPRYTLHY
RADAPLNIRSIFYVPEMKPSMFDSVALYSRKILIQTKTDILPKWLRFLRG
VVDSEDIPLNLSRELLQESALIRKLRDVLQQRVIRFLLDQSKKDPEKYAR
FFEDYGLFMREGIVTTGEQSVKEDIAKLLRFESSALPAGQQTSLMEYSSR
MKAGTRNIYYLCAPNRHLAEHSPYFEAMKQKDMEVLFCFEQFDELTLLHL
REFDRKKLISAETDIVVDHYKEEKFQDSKPASERLSSEQAEDLLAWMRNA
LVQRVTNIKVTPRLDTHPAMITVLEMGAARHFLRTQPTLEINTGHDLIKK
LHALKDSNPELAQLLLEQIYDNAMIAAGLNEDPRPMISRLNQLLTRALE
3D structure
PDB7exp Mitoquinone Inactivates Mitochondrial Chaperone TRAP1 by Blocking the Client Binding Site.
ChainB
Resolution2.297 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 05M B F368 F546 F272 F442
BS02 ANP B N134 M178 S193 G194 G214 Q215 F216 G217 V218 G219 F220 T266 R417 N50 M90 S105 G106 G118 Q119 F120 G121 V122 G123 F124 T170 R313
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7exp, PDBe:7exp, PDBj:7exp
PDBsum7exp
PubMed34758612
UniProtA0A2R8RKV0

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