Structure of PDB 7l1s Chain C

Receptor sequence
>7l1sC (length=476) Species: 2334 (Bacillus sp. PS3) [Search protein sequence]
SDVGTVIQVGDGIARAHGLDNVMSGELVEFANGVMGMALNLEENNVGIVI
LGPYTGIKEGDEVRRTGRIMEVPVGEALIGRVVNPLGQPVDGLGPVETTE
TRPIESRAPGVMDRRSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK
TSVAIDTIINQKDQNMISIYVAIGQKESTVRTVVETLRKHGALDYTIVVT
ASASQPAPLLFLAPYAGVAMGEYFMYKGKHVLVVYDDLSKQAAAYRELSL
LLRRPPGREAYPGDIFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGD
ISAYIPTNVISITDGQIFLQSDLFFSGVRPAINAGLSVSRVGGAAQIKAM
KKVAGTLRLDLAAYRELEAFAQFGSDLDKATQAKLARGARTVEVLKQDLH
QPIPVEKQVLIIYALTRGFLDDIPVEDVRRFEKEFYLFLDQNGQHLLEHI
RTTKDLPNEDDLNKAIEAFKKTFVVS
3D structure
PDB7l1s The six steps of the complete F 1 -ATPase rotary catalytic cycle.
ChainC
Resolution3.6 Å
3D
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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 C R171 Q172 T173 G174 K175 T176 F349 R354 Q422 R146 Q147 T148 G149 K150 T151 F324 R329 Q397
BS02 ATP C S336 R365 S311 R340
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7l1s, PDBe:7l1s, PDBj:7l1s
PDBsum7l1s
PubMed34344897
UniProtA0A0M3VGF9

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