Structure of PDB 6vof Chain A

Receptor sequence
>6vofA (length=496) Species: 3562 (Spinacia oleracea) [Search protein sequence]
EISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHGLDEVMAGELVEFE
EGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGR
VINALAKPIDGRGEITASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAM
IPVGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVA
QVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHT
LIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSS
LLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPA
INVGISVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKAT
QNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNGYLDSLELDQVRKY
LVELRTYVKTNKPEFQEIISSTKTFTEEAEALLKEAIQEQMERFLL
3D structure
PDB6vof Structural basis of redox modulation on chloroplast ATP synthase.
ChainA
Resolution4.51 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K176 Q201 K202 R366
Catalytic site (residue number reindexed from 1) K169 Q194 K195 R359
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 A Q173 T174 G175 K176 T177 A178 E321 F350 R355 Q423 P424 Q425 Q166 T167 G168 K169 T170 A171 E314 F343 R348 Q416 P417 Q418
BS02 ATP A V364 S365 R366 V357 S358 R359
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:0009507 chloroplast
GO:0009535 chloroplast thylakoid membrane
GO:0009579 thylakoid
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle
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:6vof, PDBe:6vof, PDBj:6vof
PDBsum6vof
PubMed32879423
UniProtP06450|ATPA_SPIOL ATP synthase subunit alpha, chloroplastic (Gene Name=atpA)

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