Structure of PDB 6ks6 Chain B

Receptor sequence

>6ks6B (length=518) Species: 559292 (Saccharomyces cerevisiae S288C)

VQIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSN
TCMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAEL
LREAEKLIDQSKIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFRED
LIHIAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGK
LSDSFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKV
DSTAKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLG
INSIEHADFEGVERLALVTGGEVVSTFDEPSKCKLGECDVIEEIMLGEQP
FLKFSGCKAGEACTIVLRGATDQTLDEAERSLHDALSVLSQTTKETRTVL
GGGCAEMVMSKAVDTEAQNIDGKKSLAVEAFARALRQLPTILADNAGFDS
SELVSKLRSSIYNGISTSGLDLNNGTIADMRQLGIVESYKLKRAVVSSAS
EAAEVLLRVDNIIRARPR

3D structure

• PDB: 6ks6 An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
• Chain: B
• Resolution: 2.99 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D59 T92 T93 D386
• Catalytic site (residue number reindexed from 1): D57 T90 T91 D384

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	B	L37 G38 P39 G91 T93 S94 S162 S163 G404 L444 I487 E489	L35 G36 P37 G89 T91 S92 S160 S161 G402 L442 I485 E487
BS02	AF3	B	D59 D90 T92 T93 K164 D386	D57 D88 T90 T91 K162 D384

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• 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:0005829 cytosol
• GO:0005832 chaperonin-containing T-complex

External links

• PDB: RCSB:6ks6, PDBe:6ks6, PDBj:6ks6
• PDBsum: 6ks6
• PubMed: 31492816
• UniProt: P39076|TCPB_YEAST T-complex protein 1 subunit beta (Gene Name=CCT2)