Structure of PDB 7tub Chain C

Receptor sequence
>7tubC (length=521) Species: 9606 (Homo sapiens) [Search protein sequence]
TPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGR
GKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAE
FLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRK
LLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGG
ALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEKDNA
EIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYF
ADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQI
GGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND
SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNA
GFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFVWEPAMVRINAL
TAASEAACLIVSVDETIKNPR
3D structure
PDB7tub Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.
ChainC
Resolution3.6 Å
3D
structure
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Enzymatic activity
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 MG C D92 A162 D89 A159
BS02 ADP C L40 D92 G93 T94 T95 S96 S164 G409 L37 D89 G90 T91 T92 S93 S161 G406
BS03 AF3 C D61 D92 T94 K166 D391 D58 D89 T91 K163 D388
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7tub, PDBe:7tub, PDBj:7tub
PDBsum7tub
PubMed36493755
UniProtQ99832|TCPH_HUMAN T-complex protein 1 subunit eta (Gene Name=CCT7)

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