Structure of PDB 7z37 Chain BP1

Receptor sequence
>7z37BP1 (length=638) Species: 9606 (Homo sapiens) [Search protein sequence]
EEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESL
TDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSG
TKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWES
SAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFI
GYPITLYLEKEREKEISKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYG
EFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNN
IKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILK
VIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLS
ELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVER
VRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKK
MEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANM
ERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVK
DLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGI
3D structure
PDB7z37 Structure of the RAF1-HSP90-CDC37 complex reveals the basis of RAF1 regulation.
ChainBP1
Resolution3.67 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 BP1 N46 A50 M93 N101 L102 G109 G127 F129 G130 G132 F133 T179 N37 A41 M84 N92 L93 G100 G118 F120 G121 G123 F124 T170
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003725 double-stranded RNA binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0019887 protein kinase regulator activity
GO:0019900 kinase binding
GO:0019901 protein kinase binding
GO:0023026 MHC class II protein complex binding
GO:0030235 nitric-oxide synthase regulator activity
GO:0030911 TPR domain binding
GO:0031072 heat shock protein binding
GO:0031625 ubiquitin protein ligase binding
GO:0042277 peptide binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0042826 histone deacetylase binding
GO:0043008 ATP-dependent protein binding
GO:0044183 protein folding chaperone
GO:0045296 cadherin binding
GO:0046983 protein dimerization activity
GO:0048156 tau protein binding
GO:0051082 unfolded protein binding
GO:0070182 DNA polymerase binding
GO:0097718 disordered domain specific binding
GO:0140662 ATP-dependent protein folding chaperone
GO:0141069 receptor ligand inhibitor activity
GO:1990226 histone methyltransferase binding
Biological Process
GO:0001890 placenta development
GO:0006457 protein folding
GO:0006986 response to unfolded protein
GO:0007004 telomere maintenance via telomerase
GO:0019062 virion attachment to host cell
GO:0030511 positive regulation of transforming growth factor beta receptor signaling pathway
GO:0031396 regulation of protein ubiquitination
GO:0032435 negative regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0032880 regulation of protein localization
GO:0034605 cellular response to heat
GO:0043066 negative regulation of apoptotic process
GO:0045429 positive regulation of nitric oxide biosynthetic process
GO:0045597 positive regulation of cell differentiation
GO:0050821 protein stabilization
GO:0051131 chaperone-mediated protein complex assembly
GO:0051726 regulation of cell cycle
GO:0060255 regulation of macromolecule metabolic process
GO:0061077 chaperone-mediated protein folding
GO:0071353 cellular response to interleukin-4
GO:0097435 supramolecular fiber organization
GO:1901799 negative regulation of proteasomal protein catabolic process
GO:1905323 telomerase holoenzyme complex assembly
GO:2000010 positive regulation of protein localization to cell surface
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0008180 COP9 signalosome
GO:0009986 cell surface
GO:0016020 membrane
GO:0032991 protein-containing complex
GO:0034751 aryl hydrocarbon receptor complex
GO:0034774 secretory granule lumen
GO:0042470 melanosome
GO:0043025 neuronal cell body
GO:0044294 dendritic growth cone
GO:0044295 axonal growth cone
GO:0048471 perinuclear region of cytoplasm
GO:0070062 extracellular exosome
GO:0101031 protein folding chaperone complex
GO:0120293 dynein axonemal particle
GO:1904813 ficolin-1-rich granule lumen
GO:1990565 HSP90-CDC37 chaperone complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:7z37, PDBe:7z37, PDBj:7z37
PDBsum7z37
PubMed36055235
UniProtP08238|HS90B_HUMAN Heat shock protein HSP 90-beta (Gene Name=HSP90AB1)

[Back to BioLiP]