Structure of PDB 4v8r Chain AD

Receptor sequence
>4v8rAD (length=515) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
NATFKNKEKPQEVRKANIIAARSVADAIRTSLGPKGMDKMIKTSRGEIII
SNDGHTILKQMAILHPVARMLVEVSAAQDSEAGDGTTSVVILTGALLGAA
ERLLNKGIHPTIIADSFQSAAKRSVDILLEMCHKVSLSDREQLVRAASTS
LSSKIVSQYSSFLAPLAVDSVLKISDENSKNVDLNDIRLVKKVGGTIDDT
EMIDGVVLTQTAIKSAGGPTRKEKAKIGLIQFQISPPKPDTENNIIVNDY
RQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLSK
LNIMVVKDIEREEIEFLSKGLGCKPIADIELFTEDRLDSADLVEEIDSDG
SKIVRVTGIPTVSVVIRGANNMIIDETERSLHDALCVIRCLVKERGLIAG
GGAPEIEISRRLSKEARSMEGVQAFIWQEFASALEVIPTTLAENAGLNSI
KVVTELRSKHENGELNDGISVRRSGTTNTYEEHILQPVLVSTSAITLASE
CVKSILRIDDIAFSR
3D structure
PDB4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
ChainAD
Resolution3.8 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 AD S38 L39 G40 P41 N59 G92 T94 S95 S160 G414 L454 S483 V484 I497 S31 L32 G33 P34 N52 G85 T87 S88 S153 G401 L441 S470 V471 I484
BS02 BEF AD N59 D91 G92 T93 T94 K161 N52 D84 G85 T86 T87 K154
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

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Biological Process
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Cellular Component
External links
PDB RCSB:4v8r, PDBe:4v8r, PDBj:4v8r
PDBsum4v8r
PubMed23478063
UniProtP39078|TCPD_YEAST T-complex protein 1 subunit delta (Gene Name=CCT4)

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