Structure of PDB 4v94 Chain L

Receptor sequence

>4v94L (length=523) Species: 559292 (Saccharomyces cerevisiae S288C)

PSNATFKNKEKPQEVRKANIIAARSVADAIRTSLGPKGMDKMIKTSRGEI
IISNDGHTILKQMAILHPVARMLVEVSAAQDSEAGDGTTSVVILTGALLG
AAERLLNKGIHPTIIADSFQSAAKRSVDILLEMCHKVSLSDREQLVRAAS
TSLSSKIVSQYSSFLAPLAVDSVLKISDENSKNVDLNDIRLVKKVGGTID
DTEMIDGVVLTQTAIKSAGGPTRKEKAKIGLIQFQISPPKPDTENNIIVN
DYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFL
SKLNIMVVKDIEREEIEFLSKGLGCKPIADIELFTEDRLDSADLVEEIDS
DGSKIVRVTGIRNNNARPTVSVVIRGANNMIIDETERSLHDALCVIRCLV
KERGLIAGGGAPEIEISRRLSKEARSMEGVQAFIWQEFASALEVIPTTLA
ENAGLNSIKVVTELRSKHENGELNDGISVRRSGTTNTYEEHILQPVLVST
SAITLASECVKSILRIDDIAFSR

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): D60 T93 T94 D396
• Catalytic site (residue number reindexed from 1): D55 T88 T89 D391

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	L	D91 S157	D86 S152
BS02	ADP	L	L39 G40 P41 D91 G92 T94 S95 T156 S160 G414 L454 I497 Q499	L34 G35 P36 D86 G87 T89 S90 T151 S155 G409 L449 I492 Q494
BS03	BEF	L	D60 D91 T93 T94 K161 D396	D55 D86 T88 T89 K156 D391

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: P39078|TCPD_YEAST T-complex protein 1 subunit delta (Gene Name=CCT4)