Structure of PDB 4j0b Chain B

Receptor sequence
>4j0bB (length=609) Species: 7955 (Danio rerio) [Search protein sequence]
TLHNIITDTENVQGSFSKHEFQAETKKLLDIVARSLYSEKEVFIRELISN
GSDALEKLRHRMITAGAPMEIHLQTDSVKGTFTIQDTGVGMNKEDLVSNL
GTIARSGSKAFLDALQSSSIIGQFGVGFYSAFMVADKVEVYSQSAEADAP
GYKWSSDGSGVFEVAEASGVRQGTKIVLHLKDDCKEFSSEDRVKEVVTKY
SNFVSFPIFLNGRRLNTLQALWMMEPKDISEWQHEEFYRYVAQAYDKPRY
TLHYRADAPLNIRSIFYVPEMKPSMFDVSREMSVALYSRKILIQTKDILP
KWLRFLRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRVIRFLLDQSK
KDPEKYARFFEDYGLFMREGIVTTGEQSVKEDIAKLLRFESSALPAGQQT
SLMEYSSRMKAGTRNIYYLCAPNRHLAEHSPYFEAMKQKDMEVLFCFEQF
DELTLLHLREFDRKKLISAETDIVVDHYKEEKFQDSKPASERLSSEQAED
LLAWMRNALVQRVTNIKVTPRLDTHPAMITVLEMGAARHFLRTILQPTLE
INTGHDLIKKLHALKDSNPELAQLLLEQIYDNAMIAAGLNEDPRPMISRL
NQLLTRALE
3D structure
PDB4j0b Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.
ChainB
Resolution2.352 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 ADP B N134 A138 M178 N186 S193 G194 S195 G214 G217 V218 G219 F220 T266 N50 A54 M91 N99 S106 G107 S108 G122 G125 V126 G127 F128 T174
BS02 BEF B G214 Q215 F216 G217 V218 G219 R417 G122 Q123 F124 G125 V126 G127 R321
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:0046872 metal ion 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:4j0b, PDBe:4j0b, PDBj:4j0b
PDBsum4j0b
PubMed24462206
UniProtA8WFV1

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