Structure of PDB 3rlr Chain A

Receptor sequence
>3rlrA (length=219) Species: 9606 (Homo sapiens) [Search protein sequence]
DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDK
IRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLG
TIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDE
QYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVK
KHSQFIGYPITLFVEKELE
3D structure
PDB3rlr Design strategies to target crystallographic waters applied to the Hsp90 molecular chaperone.
ChainA
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 3RR A L48 N51 A55 D93 M98 L107 F138 T184 V186 L40 N43 A47 D85 M90 L99 F130 T176 V178 MOAD: Ki=0.03uM
PDBbind-CN: -logKd/Ki=7.52,Ki=30nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3rlr, PDBe:3rlr, PDBj:3rlr
PDBsum3rlr
PubMed21612924
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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