Structure of PDB 4iyn Chain A

Receptor sequence
>4iynA (length=596) Species: 7955 (Danio rerio) [Search protein sequence]
TLHNIITDTENVQGSFSKHEFQAETKKLLDIVARSLYSEKEVFIRELISN
GSDALEKLRHRMITAGGDTAPMEIHLQTDSVKGTFTIQDTGVGMNKEDLV
SNLGTIARSGSKAFLDALQNQAEASSSIIGQFGVGFYSAFMVADKVEVYS
QSAEADAPGYKWSSDGSGVFEVAEASGVRQGTKIVLHLKDDCKEFSSEDR
VKEVVTKYSNFVSFPIFLNGRRLNTLQALWMMEPKDISEWQHEEFYRYVA
QAYDKPRYTLHYRADAPLNIRSIFYVPEMKPSMGSSVALYSRKILIQTKA
TDILPKWLRFLRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRVIRFL
LDQSKKDPEKYARFFEDYGLFMREGIVTTGEQSVKEDIAKLLRFESSALP
AGQQTSLMEYSSRMKAGTRNIYYLCAPNRHLAEHSPYFEAMKQKDMEVLF
CFEQFDELTLLHLREFDRKKLISAETRLSSEQAEDLLAWMRNALVQRVTN
IKVTPRLDTHPAMITVLEMGAARHFLRTQQLQPTLEINTGHDLIKKLHAL
KDSNPELAQLLLEQIYDNAMIAAGLNEDPRPMISRLNQLLTRALEK
3D structure
PDB4iyn Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.
ChainA
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 A N134 M178 N186 S193 G194 S195 G214 G217 V218 G219 F220 T266 N50 M94 N102 S109 G110 S111 G130 G133 V134 G135 F136 T182
BS02 ALF A E130 F216 G217 V218 G219 R417 E46 F132 G133 V134 G135 R326
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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