Structure of PDB 7trg Chain C

Receptor sequence
>7trgC (length=521) Species: 9606 (Homo sapiens) [Search protein sequence]
TPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGR
GKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAE
FLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRK
LLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGG
ALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEKDNA
EIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYF
ADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQI
GGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND
SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNA
GFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFVWEPAMVRINAL
TAASEAACLIVSVDETIKNPR
3D structure
PDB7trg Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.
ChainC
Resolution3.0 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 P42 D92 G93 T95 S164 S165 G409 R510 L37 P39 D89 G90 T92 S161 S162 G406 R496
BS02 AF3 C N60 D61 K166 D391 N57 D58 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:7trg, PDBe:7trg, PDBj:7trg
PDBsum7trg
PubMed36493755
UniProtQ99832|TCPH_HUMAN T-complex protein 1 subunit eta (Gene Name=CCT7)

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