Structure of PDB 7ykk Chain B

Receptor sequence

>7ykkB (length=735) Species: 4932 (Saccharomyces cerevisiae)

FKLPAEFITRPHPSKDHGKETCTAYIHPNVLSSLEINPGSFCTVGKIGEN
GILVIARAGDEEVHPVNVITLSTTIRSVGNLILGDRLELKKAQVQPPYAT
KVTVGSLQGYNILECMEEKVIQKLLDDSGVIMPGMIFQNLKTKAGDESID
VVITDASDDSLPDVSQLDLNMDDMYGGLGSTHITFSKETQANRKYNLPEP
LSYAAVGGLDKEIESLKSAIEIPLHQPTLFSSFGVSPPRGILLHGPPGTG
KTMLLRVVANTSNAHVLTINGPSIVSKYLGETEAALRDIFNEARKYQPSI
IFIDEIDSIAPNRANDDSGEVESRVVATLLTLMDGMGAAGKVVVIAATNR
PNSVDPALRRPGRFDQEVEIGIPDVDARFDILTKQFSRMSSDRHVLDSEA
IKYIASKTHGYVGADLTALCRESVMKTIQRGLGTDANIDKFSLKVTLKDV
ESAMVDIRPSAMREIFLEMPKVYWSDIGGQEELKTKMKEMIQLPLEASET
FARLGISAPKGVLLYGPPGCSKTLTAKALATESGINFLAVKGPEIFNKYV
GESERAIREIFRKARSAAPSIIFFDEIDALSPDRDGSSTSAANHVLTSLL
NEIDGVEELKGVVIVAATNRPDEIDAALLRPGRLDRHIYVGPPDVNARLE
ILKKCTKKFNTEESGVDLHELADRTEGYSGAEVVLLCQEAGLAAIMEDLD
VAKVELRHFEKAFKGIARGITPEMLSYYEEFALRS

3D structure

• PDB: 7ykk Structural dynamics of AAA + ATPase Drg1 and mechanism of benzo-diazaborine inhibition.
• Chain: B
• Resolution: 5.9 Å

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	B	G289 T290 G291 K292 T293 M294 G454 A455 T458	G248 T249 G250 K251 T252 M253 G413 A414 T417

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

External links

• PDB: RCSB:7ykk, PDBe:7ykk, PDBj:7ykk
• PDBsum: 7ykk
• PubMed: 36351914
• UniProt: P32794|AFG2_YEAST ATPase family gene 2 protein (Gene Name=AFG2)