Structure of PDB 7ykk Chain D

Receptor sequence
>7ykkD (length=734) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
FKLPAEFITRPHPSKDHGKECTAYIHPNVLSSLEINPGSFCTVGKIGENG
ILVIARAGDEEVHPVNVITLSTTIRSVGNLILGDRLELKKAQVQPPYATK
VTVGSLQGYNILECMEEKVIQKLLDDSGVIMPGMIFQNLKTKAGDESIDV
VITDASDDSLPDVSQLDLNMDDMYGGLGSTHITFSKETQANRKYNLPEPL
SYAAVGGLDKEIESLKSAIEIPLHQPTLFSSFGVSPPRGILLHGPPGTGK
TMLLRVVANTSNAHVLTINGPSIVSKYLGETEAALRDIFNEARKYQPSII
FIDEIDSIAPNRANDDSGEVESRVVATLLTLMDGMGAAGKVVVIAATNRP
NSVDPALRRPGRFDQEVEIGIPDVDARFDILTKQFSRMSSDRHVLDSEAI
KYIASKTHGYVGADLTALCRESVMKTIQRGLGTDANIDKFSLKVTLKDVE
SAMVDIRPSAMREIFLEMPKVYWSDIGGQEELKTKMKEMIQLPLEASETF
ARLGISAPKGVLLYGPPGCSKTLTAKALATESGINFLAVKGPEIFNKYVG
ESERAIREIFRKARSAAPSIIFFDEIDALSPDRDGSSTSAANHVLTSLLN
EIDGVEELKGVVIVAATNRPDEIDAALLRPGRLDRHIYVGPPDVNARLEI
LKKCTKKFNTEESGVDLHELADRTEGYSGAEVVLLCQEAGLAAIMEDLDV
AKVELRHFEKAFKGIARGITPEMLSYYEEFALRS
3D structure
PDB7ykk Structural dynamics of AAA + ATPase Drg1 and mechanism of benzo-diazaborine inhibition.
ChainD
Resolution5.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
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 ATP D T290 K292 T293 M294 I422 G454 A455 T458 T248 K250 T251 M252 I380 G412 A413 T416
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0009410 response to xenobiotic stimulus
GO:0034214 protein hexamerization
GO:0042254 ribosome biogenesis
GO:0042273 ribosomal large subunit biogenesis
Cellular Component
GO:0005737 cytoplasm
GO:0030687 preribosome, large subunit precursor

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7ykk, PDBe:7ykk, PDBj:7ykk
PDBsum7ykk
PubMed36351914
UniProtP32794|AFG2_YEAST ATPase family gene 2 protein (Gene Name=AFG2)

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