Structure of PDB 5lqz Chain E

Receptor sequence
>5lqzE (length=469) Species: 870730 (Ogataea angusta) [Search protein sequence]
PASGKIRAVIGAVVDVQFEQGELPAILNALTIDQGNNQKLVLEVAQHLGE
NAVRAIAMDGTEGLVRGQTVVDTGAPISVPVGRGTLGRIINVVGEPIDER
GPIECKQRNPIHADPPSFVEQSTEAEVLETGIKVVDLLAPYARGGKIGLF
GGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGV
INLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFVD
NIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTRKGSVTS
VQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSR
LLDVSVVGQEHYDVATGVQQTLQAYKSLQDIIAILGMDELSEQDKLTVER
ARKIQRFLSQPFAVAEVFTGIEGKLVRLKDTIASFKAVLEGKYDHLPENA
FYMVGGIEDVVAKAEKIAA
3D structure
PDB5lqz Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy.
ChainE
Resolution7.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G161 G187 V188 S354
Catalytic site (residue number reindexed from 1) G154 G180 V181 S347
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 E A160 G161 G163 K164 T165 V166 Y346 A422 A153 G154 G156 K157 T158 V159 Y339 A415
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
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:0016020 membrane
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:5lqz, PDBe:5lqz, PDBj:5lqz
PDBsum5lqz
PubMed27791192
UniProtW1QA59

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