Structure of PDB 4v94 Chain N

Receptor sequence

>4v94N (length=538) Species: 559292 (Saccharomyces cerevisiae S288C)

SLQLLNPKAESLRRDAALKVNVTSAEGLQSVLETNLGPKGTLKMLVDGAG
NIKLTKDGKVLLTEMQIQSPTAVLIARAAAAQDEITGDGTTTVVCLVGEL
LRQAHRFIQEGVHPRIITDGFEIARKESMKFLDEFKISKTNLSNDREFLL
QVARSSLLTKVDADLTEVLTPIVTDAVLSVYDAQADNLDLHMVEIMQMQH
LSPKDTTFIKGLVLDHGGRHPDMPTRVKNAYVLILNVSLEYEKTEVNSGF
FYSSADQRDKLAASERKFVDAKLKKIIDLKNEVCGMDPDKGFVIINQKGI
DPMSLDVFAKHNILALRRAKRRNMERLQLVTGGEAQNSVEDLSPQILGFS
GLVYQETIGEEKFTYVTENTDPKSCTILIKGSTHYALAQTKDAVRDGLRA
VANVLKDKNIIPGAGAFYIALSRYLRSANMNKLGAKGKTKTGIEAFAEAL
LVIPKTLVKNSGFDPLDVLAMVEDELDDAQDSDETRYVGVDLNIGDSCDP
TIEGIWDSYRVLRNAITGATGIASNLLLCDELLRAGRS

3D structure

• PDB: 4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
• Chain: N
• Resolution: 3.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D58 T91 T92 D397
• Catalytic site (residue number reindexed from 1): D57 T90 T91 D396

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	N	D89 T160	D88 T159
BS02	ADP	N	L37 G38 D89 G90 T93 T160 A415 L458 L493 I506	L36 G37 D88 G89 T92 T159 A414 L457 L492 I505
BS03	BEF	N	D58 T91 T92 K161	D57 T90 T91 K160

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
• GO:0051086 chaperone mediated protein folding independent of cofactor

Cellular Component

• GO:0005737 cytoplasm
• GO:0005832 chaperonin-containing T-complex

External links

• PDB: RCSB:4v94, PDBe:4v94, PDBj:4v94
• PDBsum: 4v94
• PubMed: 22503819
• UniProt: P39079|TCPZ_YEAST T-complex protein 1 subunit zeta (Gene Name=CCT6)