Structure of PDB 3rlp Chain B

Receptor sequence
>3rlpB (length=218) Species: 9606 (Homo sapiens) [Search protein sequence]
DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDK
IRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLG
TITKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAW
ESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQ
FIGYPITLFVEKELEHHH
3D structure
PDB3rlp Design strategies to target crystallographic waters applied to the Hsp90 molecular chaperone.
ChainB
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
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 3RP B S52 A55 G97 M98 L107 F138 S44 A47 G89 M90 L99 F126 MOAD: Kd=0.084uM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3rlp, PDBe:3rlp, PDBj:3rlp
PDBsum3rlp
PubMed21612924
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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