Structure of PDB 1e1q Chain A

Receptor sequence
>1e1qA (length=487) Species: 9913 (Bos taurus) [Search protein sequence]
DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGV
VVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGS
KARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQT
GKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA
DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSK
QAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTA
LPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR
VGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR
LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVI
SQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA
3D structure
PDB1e1q Structure of Bovine Mitochondrial F1-ATPase Inhibited by Mg2+Adp and Aluminium Fluoride
ChainA
Resolution2.61 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q208 K209 R373
Catalytic site (residue number reindexed from 1) K152 Q185 K186 R350
Enzyme Commision number 3.6.1.34: 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 A R171 Q172 G174 K175 T176 S177 F357 R362 P363 Q432 R148 Q149 G151 K152 T153 S154 F334 R339 P340 Q409
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
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:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005886 plasma membrane
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)
GO:0045267 proton-transporting ATP synthase, catalytic core

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1e1q, PDBe:1e1q, PDBj:1e1q
PDBsum1e1q
PubMed10873854
UniProtP19483|ATPA_BOVIN ATP synthase subunit alpha, mitochondrial (Gene Name=ATP5F1A)

[Back to BioLiP]