Structure of PDB 6xhj Chain A

Receptor sequence
>6xhjA (length=473) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence]
GSSRTYGKEALRANIAAVKAIEEALKSTYGPRGMDKMLVDSLGDITITND
GATILDKMDLQHPTGKLLVQIAKGQDEETADGTKTAVILAGELAKKAEDL
LYKEIHPTIIVSGYKKAEEIALKTIQEIAQPVTINDTDVLRKVALTSLGS
KAVAGAREYLADLVVKAVAQVAELRGDKWYVDLDNVQIVKKHGGSVNDTQ
LVYGIVVDKEVVHPGMPKRIENAKIALLDAPTQMHKFLEEEENILKEKVD
KIAATGANVVICQKVAQHYLAKLAVRRSDLEKLARATGGRVELDLGYAAL
VEERKDKMVFVEGAKNPKSVSILIRGGLERVVDETERALRDALGTVADVI
RDGRAVAGGGAVEIEIAKRLRKYAPQVGGKEQLAIEAYANAIEGLIMILA
ENAGLDPIDKLMQLRSLHENETNKWYGLNLFTGNPEDMWKLGVIEPALVK
MNAVKAATEAVTLVLRIDDIVAA
3D structure
PDB6xhj Structural analysis of the Sulfolobus solfataricus TF55beta chaperonin by cryo-electron microscopy
ChainA
Resolution3.62 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D70 T103 K104 D399
Catalytic site (residue number reindexed from 1) D50 T83 K84 D341
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 A G50 P51 D101 G102 T103 K104 G417 V501 G30 P31 D81 G82 T83 K84 G359 V443
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:6xhj, PDBe:6xhj, PDBj:6xhj
PDBsum6xhj
PubMed
UniProtQ9V2T8|THSB_SACS2 Thermosome subunit beta (Gene Name=thsB)

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