Structure of PDB 5njx Chain A Binding Site BS01

Receptor Information
>5njx Chain A (length=413) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLS
NGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYA
YGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNP
NEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQRE
EQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTK
EKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKAS
ESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQL
LMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANM
FKKFAEQDAKEEA
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5njx Combined x-ray crystallography and computational modeling approach to investigate the Hsp90 C-terminal peptide binding to FKBP51.
Resolution2.49 Å
Binding residue
(original residue number in PDB)		K272 T276 N322 K329 E351 K352 Y355 R356 N384 A386
Binding residue
(residue number reindexed from 1)		K260 T264 N310 K317 E339 K340 Y343 R344 N372 A374
Enzymatic activity
Catalytic site (original residue number in PDB) Y57 F67 D68 I87 Y113 F130
Catalytic site (residue number reindexed from 1) Y45 F55 D56 I75 Y101 F118
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0005528 FK506 binding
GO:0030674 protein-macromolecule adaptor activity
GO:0031072 heat shock protein binding
Biological Process
GO:0006457 protein folding
GO:0009617 response to bacterium
GO:0042220 response to cocaine
GO:0061077 chaperone-mediated protein folding
GO:0097305 response to alcohol
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5njx, PDBe:5njx, PDBj:5njx
PDBsum5njx
PubMed29079741
UniProtQ13451|FKBP5_HUMAN Peptidyl-prolyl cis-trans isomerase FKBP5 (Gene Name=FKBP5)

[Back to BioLiP]