Structure of PDB 8spx Chain B

Receptor sequence
>8spxB (length=474) Species: 2334 (Bacillus sp. PS3) [Search protein sequence]
SDVGTVIQVGDGIARAHGLDNVMSGELVEFANGVMGMALNLEENNVGIVI
LGPYTGIKEGDEVRRTGRIMEVPVGEALIGRVVNPLGQPVDGLGPVETTE
TRPIESRAPGVMDRRSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK
TSVAIDTIINQKDQNMISIYVAIGQKESTVRTVVETLRKHGALDYTIVVT
ASASQPAPLLFLAPYAGVAMGEYFMYKGKHVLVVYDDLSKQAAAYRELSL
LLRRPPGREAYPGDIFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGD
ISAYIPTNVISITDGQIFLQSDLFFSGVRPAINAGLSVSRVGGAAQIKAM
KKVAGTLRLDLAAYRELEAFAQFGSDLDKATQAKLARGARTVEVLKQDLH
QPIPVEKQVLIIYALTRGFLDDIPVEDVRRFEKEFYLFLDQNGQHLLEHI
RTTKDLPNEDDLNKAIEAFKKTFV
3D structure
PDB8spx PS3 F1 Rotorless
ChainB
Resolution2.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector 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 R171 Q172 G174 K175 T176 S177 F349 R354 R146 Q147 G149 K150 T151 S152 F324 R329
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Cellular Component
External links
PDB RCSB:8spx, PDBe:8spx, PDBj:8spx
PDBsum8spx
PubMed38237595
UniProtA0A0M3VGF9

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