Structure of PDB 6n2y Chain C

Receptor sequence
>6n2yC (length=494) Species: 2334 (Bacillus sp. PS3) [Search protein sequence]
ISALIKQQIENYESQIQVSDVGTVIQVGDGIARAHGLDNVMSGELVEFAN
GVMGMALNLEENNVGIVILGPYTGIKEGDEVRRTGRIMEVPVGEALIGRV
VNPLGQPVDGLGPVETTETRPIESPAPGVMDRRSVHEPLQTGIKAIDALV
PIGRGQRELIIGDRQTGKTSVAIDTIINQKDQNMISIYVAIGQKESTVRT
VVETLRKHGALDYTIVVTASASQPAPLLFLAPYAGVAMGEYFMYKGKHVL
VVYDDLSKQAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSDA
KGGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAI
NAGLSVSRVGGAAQIKAMKKVAGTLRLDLAAYRELEAFAQFGSDLDKATQ
AKLARGARTVEVLKQDLHQPIPVEKQVLIIYALTRGFLDDIPVEDVRRFE
KEFYLFLDQNGQHLLEHIRTTKDLPNEDDLNKAIEAFKKTFVVS
3D structure
PDB6n2y Structure of a bacterial ATP synthase.
ChainC
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q200 K201 R365
Catalytic site (residue number reindexed from 1) K168 Q193 K194 R358
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 Q172 G174 K175 T176 S177 F349 R354 L424 Q165 G167 K168 T169 S170 F342 R347 L417
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:6n2y, PDBe:6n2y, PDBj:6n2y
PDBsum6n2y
PubMed30724163
UniProtA0A0M3VGF9

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