Structure of PDB 3j1f Chain R

Receptor sequence
>3j1fR (length=505) Species: 146920 (Acidianus tengchongensis) [Search protein sequence]
GKEAVRANIAAVKAVEEALKSTYGPRGMDKMLVDSLGDITITNDGATILD
KMDLQHPAAKLLVQIAKGQDEETADGTKTAVIFSGELVKKAEDLLYKDVH
PTIIISGYKKAEEVALQTIQELAQTVSINDTDLLRKIAMTSLSSKAVAGA
REYIADIVVKAVTQVAELRGDKWYVDLDNIQIVKKAGGSINDTQLVYGIV
VDKEVVHPGMPKRLENAKIALIDASLEVEKPELDAEIRINDPTQMQKFLD
EEENLIKEKVDKILATGANVIICQKGIDEVAQSYLAKKGVLAVRRAKKSD
LEKLARATGGRVVSNIDEISEQDLGYASLIEERKVGEDKMVFVEGAKNPK
SISILIRGGLERLVDETERALRDALGTVADVIKDGRAIAGGGAVEIEIAK
KLRKYAPQVGGKEQLAVEAYANALESLVSILIENAGFDPIDLLMKLRSTH
ENENNKWYGIDLYAGQPVDMWQKGVIEPALVKMNAIKAATEAATLVLRID
DVVSA
3D structure
PDB3j1f Flexible interwoven termini determine the thermal stability of thermosomes.
ChainR
Resolution6.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D71 T104 K105 D400
Catalytic site (residue number reindexed from 1) D44 T77 K78 D373
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 R Y50 G51 P52 D102 G103 T104 K105 T106 G417 G418 L489 M497 E504 K509 Y23 G24 P25 D75 G76 T77 K78 T79 G390 G391 L462 M470 E477 K482
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
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:3j1f, PDBe:3j1f, PDBj:3j1f
PDBsum3j1f
PubMed23709365
UniProtQ877H2

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