Structure of PDB 6vog Chain F

Receptor sequence
>6vogF (length=478) Species: 3562 (Spinacia oleracea) [Search protein sequence]
KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAGQPMNVTCEVQ
QLLGNNRVRAVAMSATDGLTRGMEVIDTGAPLSVPVGGATLGRIFNVLGE
PVDNLGPVDTRTTSPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGG
KIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM
KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQ
DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITST
KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD
PLDSTSTMLQPRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE
DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGEL
DSLPEQAFYLVGNIDEATAKAMNLEMES
3D structure
PDB6vog Structural basis of redox modulation on chloroplast ATP synthase.
ChainF
Resolution4.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K178 E204 R205 T373
Catalytic site (residue number reindexed from 1) K162 E188 R189 T357
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 F T373 Q376 T357 Q360
BS02 ATP F G175 V176 G177 K178 T179 V180 R205 Y362 G159 V160 G161 K162 T163 V164 R189 Y346
Gene Ontology
Molecular Function
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:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0009507 chloroplast
GO:0009535 chloroplast thylakoid membrane
GO:0009579 thylakoid
GO:0016020 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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Cellular Component
External links
PDB RCSB:6vog, PDBe:6vog, PDBj:6vog
PDBsum6vog
PubMed32879423
UniProtP00825|ATPB_SPIOL ATP synthase subunit beta, chloroplastic (Gene Name=atpB)

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