Structure of PDB 3j1f Chain B

Receptor sequence
>3j1fB (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.
ChainB
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 B Y50 P52 D102 G103 T104 K105 T106 G418 L489 E504 K509 Y23 P25 D75 G76 T77 K78 T79 G391 L462 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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