Structure of PDB 7ttn Chain C

Receptor sequence
>7ttnC (length=521) Species: 9606 (Homo sapiens) [Search protein sequence]
TPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGR
GKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAE
FLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRK
LLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGG
ALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEKDNA
EIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYF
ADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQI
GGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND
SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNA
GFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFVWEPAMVRINAL
TAASEAACLIVSVDETIKNPR
3D structure
PDB7ttn Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.
ChainC
Resolution3.3 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 ADP C L40 D92 G93 T94 T95 S165 G409 V502 L37 D89 G90 T91 T92 S162 G406 V489
BS02 AF3 C D61 G62 T94 K166 D391 D58 G59 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
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Biological Process
External links
PDB RCSB:7ttn, PDBe:7ttn, PDBj:7ttn
PDBsum7ttn
PubMed36493755
UniProtQ99832|TCPH_HUMAN T-complex protein 1 subunit eta (Gene Name=CCT7)

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