Structure of PDB 7l1q Chain D

Receptor sequence
>7l1qD (length=470) Species: 2334 (Bacillus sp. PS3) [Search protein sequence]
TRGRVIQVMGPVVDVKFENGHLPAIYNALKIQHKARNENEVDIDLTLEVA
LHLGDDTVRTIAMASTDGLIRGMEVIDTGAPISVPVGEVTLGRVFNVLGE
PIDLEGDIPADARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKG
GKIGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGDRTREGNDLYHE
MKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFI
DNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTAKGSIT
SIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTS
RALAPEIVGEEHYQVARKVQQTLQRYKELQDIIAILGMDELSDEDKLVVH
RARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILEGKYDHLPED
AFRLVGRIEEVVEKAKAMGV
3D structure
PDB7l1q The six steps of the complete F 1 -ATPase rotary catalytic cycle.
ChainD
Resolution3.4 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 ADP D G163 T165 V166 G162 T164 V165
BS02 PO4 D K164 R191 N253 R256 K163 R190 N252 R255
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
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:7l1q, PDBe:7l1q, PDBj:7l1q
PDBsum7l1q
PubMed34344897
UniProtP07677|ATPB_BACP3 ATP synthase subunit beta (Gene Name=atpD)

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