Structure of PDB 7ylw Chain b

Receptor sequence
>7ylwb (length=518) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
VQIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSN
TCMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAEL
LREAEKLIDQSKIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFRED
LIHIAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGK
LSDSFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKV
DSTAKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLG
INSIEHADFEGVERLALVTGGEVVSTFDEPSKCKLGECDVIEEIMLGEQP
FLKFSGCKAGEACTIVLRGATDQTLDEAERSLHDALSVLSQTTKETRTVL
GGGCAEMVMSKAVDTEAQNIDGKKSLAVEAFARALRQLPTILADNAGFDS
SELVSKLRSSIYNGISTSGLDLNNGTIADMRQLGIVESYKLKRAVVSSAS
EAAEVLLRVDNIIRARPR
3D structure
PDB7ylw Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Chainb
Resolution3.39 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 b D90 S162 G404 I487 E489 D88 S160 G402 I485 E487
BS02 AF3 b D59 D90 G91 T92 K164 D386 D57 D88 G89 T90 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7ylw, PDBe:7ylw, PDBj:7ylw
PDBsum7ylw
PubMed36921056
UniProtP39076|TCPB_YEAST T-complex protein 1 subunit beta (Gene Name=CCT2)

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