Structure of PDB 4iyn Chain B

Receptor sequence
>4iynB (length=609) Species: 7955 (Danio rerio) [Search protein sequence]
TLHNIITDTENVQGSFSKHEFQAETKKLLDIVARSLYSEKEVFIRELISN
GSDALEKLRHRMITTAPMEIHLQTDSVKGTFTIQDTGVGMNKEDLVSNLG
TIARSGSKAFLDALQASSSIIGQFGVGFYSAFMVADKVEVYSQSAEADAP
GYKWSSDGSGVFEVAEASGVRQGTKIVLHLKDDCKEFSSEDRVKEVVTKY
SNFVSFPIFLNGRRLNTLQALWMMEPKDISEWQHEEFYRYVAQAYDKPRY
TLHYRADAPLNIRSIFYVPEMKPSMFDVSREMSSVALYSRKILIQTDILP
KWLRFLRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRVIRFLLDQSK
KDPEKYARFFEDYGLFMREGIVTTGEQSVKEDIAKLLRFESSALPAGQQT
SLMEYSSRMKAGTRNIYYLCAPNRHLAEHSPYFEAMKQKDMEVLFCFEQF
DELTLLHLREFDRKKLISAETDIVVDHYKEEKFQDSKPASERLSSEQAED
LLAWMRNALVQRVTNIKVTPRLDTHPAMITVLEMGAARHFLRTILQPTLE
INTGHDLIKKLHALKDSNPELAQLLLEQIYDNAMIAAGLNEDPRPMISRL
NQLLTRALE
3D structure
PDB4iyn Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.
ChainB
Resolution2.312 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 M90 N98 S105 G106 S107 G122 G125 V126 G127 F128 T174
BS02 ALF B E130 G214 F216 G217 V218 G219 R417 E46 G122 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:4iyn, PDBe:4iyn, PDBj:4iyn
PDBsum4iyn
PubMed24462206
UniProtA8WFV1

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