Structure of PDB 3ko1 Chain E

Receptor sequence
>3ko1E (length=505) Species: 146920 (Acidianus tengchongensis) [Search protein sequence]
GKEAVRANIAAVKAVEEALKSTYGPRGMDKMLVDSLGDITITNDGATILD
KMDLQHPAAKLLVQIAKGQDEETADGTKTAVIFSGELVKKAEDLLYKDVH
PTIIISGYKKAEEVALQTIQELAQTVSINDTDLLRKIAMTSLSSKAVAGA
REYIADIVVKAVTQVAELRGDKWYVDLDNIQIVKKAGGSINDTQLVYGIV
VDKEVVHPGMPKRLENAKIALIDASLEVEKPELDAEIRINDPTQMQKFLD
EEENLIKEKVDKILATGANVIICQKGIDEVAQSYLAKKGVLAVRRAKKSD
LEKLARATGGRVVSNIDEISEQDLGYASLIEERKVGEDKMVFVEGAKNPK
SISILIRGGLERLVDETERALRDALGTVADVIKDGRAIAGGGAVEIEIAK
KLRKYAPQVGGKEQLAVEAYANALESLVSILIENAGFDPIDLLMKLRSTH
ENENNKWYGIDLYAGQPVDMWQKGVIEPALVKMNAIKAATEAATLVLRID
DVVSA
3D structure
PDB3ko1 Crystal structure of group II chaperonin in the open state.
ChainE
Resolution3.7 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 ADP E Y50 G51 G103 K105 T106 S171 G417 G418 V502 E504 K509 Y23 G24 G76 K78 T79 S144 G390 G391 V475 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:3ko1, PDBe:3ko1, PDBj:3ko1
PDBsum3ko1
PubMed20947016
UniProtQ877H2

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