Structure of PDB 5lqz Chain D

Receptor sequence
>5lqzD (length=471) Species: 870730 (Ogataea angusta) [Search protein sequence]
AGPASGKIRAVIGAVVDVQFEQGELPAILNALTIDQGNNQKLVLEVAQHL
GENAVRAIAMDGTEGLVRGQTVVDTGAPISVPVGRGTLGRIINVVGEPID
ERGPIECKQRNPIHADPPSFVEQSTEAEVLETGIKVVDLLAPYARGGKIG
LFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKET
GVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLF
VDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTRKGSV
TSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSK
SRLLDVSVVGQEHYDVATGVQQTLQAYKSLQDIIAILGMDELSEQDKLTV
ERARKIQRFLSQPFAVAEVFTGIEGKLVRLKDTIASFKAVLEGKYDHLPE
NAFYMVGGIEDVVAKAEKIAA
3D structure
PDB5lqz Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy.
ChainD
Resolution7.0 Å
3D
structure
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Enzymatic activity
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 D A160 G161 G163 T165 V166 Y346 A422 A155 G156 G158 T160 V161 Y341 A417
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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Biological Process
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Cellular Component
External links
PDB RCSB:5lqz, PDBe:5lqz, PDBj:5lqz
PDBsum5lqz
PubMed27791192
UniProtW1QA59

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