Structure of PDB 8u1m Chain B

Receptor sequence
>8u1mB (length=494) Species: 7111 (Trichoplusia ni) [Search protein sequence]
GEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESL
TDPSKLDSGKELYIKIIPNKSEGTFTIIDTGIGMTKADLVNNLGTIAKSG
TKAFMEALQAGADISMIGQFGVGFYSCYLVADRVTVHSKHNDDEQYMWES
SAGGSFTVRTDHGEPLGRGTKIVLHIKEDLAEYLEVNKIKEIVKKHSQFI
GYPIKLTVEKEREKEKKKTIKEKYTEDEELNKTKPIWTRNADDITQEEYG
DFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENKKRKNN
IKLYVRRVFIMDNCEDLIPEYLNFIKGVVDSEDLPLNISREMLQQNKILK
VIRKNLVKKCLELFEELAEDKENYKKYYEQFSKNLKLGIHEDAQNRTKLA
DLLRYHTSASGDEACSLKEYVSRMKENQKHIYYITGENRDQVANSSFVER
VKKRGYEVVYMTEPIDEYVVQQMREYDGKTLVSVTKEGLELPED
3D structure
PDB8u1m Structural dynamics of RAF1-HSP90-CDC37 and HSP90 complexes reveal asymmetric client interactions and key structural elements.
ChainB
Resolution3.5 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 ATP B E42 S45 N46 S47 A50 M93 N101 L102 S108 G109 I126 G127 F129 G130 V131 G132 F133 R391 E33 S36 N37 S38 A41 M84 N92 L93 S99 G100 I117 G118 F120 G121 V122 G123 F124 R340
BS02 MG B E42 N46 E33 N37
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0097718 disordered domain specific binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0034605 cellular response to heat
GO:0050821 protein stabilization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0032991 protein-containing complex
GO:0048471 perinuclear region of cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8u1m, PDBe:8u1m, PDBj:8u1m
PDBsum8u1m
PubMed38431713
UniProtA0A7E5VSK5

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