Structure of PDB 3oeh Chain T

Receptor sequence
>3oehT (length=479) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
NLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGI
VLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDA
AGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQT
GKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQH
DAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSK
QAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTA
LPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSR
VGSAAQVKALKQVAGSLKLFLAQYREVAAFALDASTKQTLVRGERLTQLL
KQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNE
LLTEIREKGELSKELLASLKSATESFVAT
3D structure
PDB3oeh Crystal structures of mutant forms of the yeast f1 ATPase reveal two modes of uncoupling.
ChainT
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) K177 Q210 K211 R375
Catalytic site (residue number reindexed from 1) K152 Q185 K186 R350
Enzyme Commision number 3.6.3.14: Transferred entry: 7.1.2.2.
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 ANP T Q174 T175 G176 K177 T178 A179 R364 Q432 Q434 Q149 T150 G151 K152 T153 A154 R339 Q402 Q404
BS02 ANP T S346 V373 R375 S321 V348 R350
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
GO:0046933 proton-transporting ATP synthase 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:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005758 mitochondrial intermembrane space
GO:0005829 cytosol
GO:0016020 membrane
GO:0042645 mitochondrial nucleoid
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)
GO:0045267 proton-transporting ATP synthase, catalytic core

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3oeh, PDBe:3oeh, PDBj:3oeh
PDBsum3oeh
PubMed20843806
UniProtP07251|ATPA_YEAST ATP synthase subunit alpha, mitochondrial (Gene Name=ATP1)

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