Structure of PDB 7wbb Chain F

Receptor sequence
>7wbbF (length=699) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
KLPAEFITRPHPSKDHGKETCTAYIHPNVLSSLEINPGSFCTVGKIGENG
ILVIARAGDEEVHPVNVITLSTTIRSVGNLILGDRLELKKAQVQPPYATK
VTVGSLQGYNILECMEEKVIQKLLDDSGVIMPGMIFQNLKTKAGDESIDV
VITDASDFYLSPPFIFRKGSTHITFSKETQANRKYNLPEPLSYAAVGGLD
KEIESLKSAIEIPLHQPTLFSSFGVSPPRGILLHGPPGTGKTMLLRVVAN
TSNAHVLTINGPSIVSKYLGETEAALRDIFNEARKYQPSIIFIDQIDSIA
PNRANDDSGEVESRVVATLLTLMDGMGAAGKVVVIAATNRPNSVDPALRR
PGRFDQEVEIGIPDVDARFDILTKQFSRMSSDRHVLDSEAIKYIASKTHG
YVGADLTALCRESVMKTIQRGLGTDANIDKFSLKVTLKDVESAMVDIRPS
AMRVYWSDIGGQEELKTKMKEMIQLPLEASETFARLGISAPKGVLLYGPP
GCSKTLTAKALATESGINFLAVKGPEREIFRKARSAAPSIIFFDQIDALS
PTSAANHVLTSLLNEIDGVEELKGVVIVAATNRPDEIDAALLRPGRLDRH
IYVGPPDVNARLEILKKCTKKFNTEESGVDLHELADRTEGYSGAEVVLLC
QEAGLAAIMEDLDVAKVELRHFEKAFKGIARGITPEMLSYYEEFALRSG
3D structure
PDB7wbb Structural dynamics of AAA + ATPase Drg1 and mechanism of benzo-diazaborine inhibition.
ChainF
Resolution3.6 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 F G248 G289 T290 G291 K292 T293 M294 I422 G197 G238 T239 G240 K241 T242 M243 I371
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:7wbb, PDBe:7wbb, PDBj:7wbb
PDBsum7wbb
PubMed36351914
UniProtP32794|AFG2_YEAST ATPase family gene 2 protein (Gene Name=AFG2)

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