Structure of PDB 6gpp Chain A

Receptor sequence
>6gppA (length=232) Species: 9606 (Homo sapiens) [Search protein sequence]
VPRGSHMPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIF
LRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDT
GIGMTKADLINNLGTIAASGTKAFMEALQAGADISMIGQFGVGFYSAYLV
AEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQ
TEYLEERRIKEIVKKHSQFIGYPITLFVEKER
3D structure
PDB6gpp Probing the role of Arg97 in Heat shock protein 90 N-terminal domain from the parasite Leishmania braziliensis through site-directed mutagenesis on the human counterpart.
ChainA
Resolution1.51 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 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 ADP A N51 A55 M98 G137 F138 T184 N57 A61 M104 G143 F144 T190
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:6gpp, PDBe:6gpp, PDBj:6gpp
PDBsum6gpp
PubMed30248409
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

[Back to BioLiP]