Structure of PDB 5fl7 Chain D

Receptor sequence
>5fl7D (length=470) Species: 4952 (Yarrowia lipolytica) [Search protein sequence]
GVGSGKIRTVIGAVVDVQFEQDNLPAILNALTIDRGEGNKLVLEVAQHLG
ENTVRTIAMDGTEGLVRGTSVADTGAPITIPVGRGTLGRIINVCGEPIDE
RGPIEATKFLPIHADPPTFAEQSTTAEVLETGIKVVDLLAPYARGGKIGL
FGGAGVGKTVFIQELINNIAKAHGGFSVFCGVGERTREGNDLYREMKETG
VINLEGESKVTLVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFV
DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGALQERITTTQKGSVT
SVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKS
RLLDIDVVGQEHYDVASNVQQTLQAYKSLQDIIAILGMDELSEQDKLTVE
RARKIQRFLSQPFTVAEVFTGIEGRLVSLKDTVRSFKEILDGKHDALPEA
AFYMVGGIEEVVAKAEKLAA
3D structure
PDB5fl7 Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology.
ChainD
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K194 E220 R221 R387
Catalytic site (residue number reindexed from 1) K158 E184 R185 R351
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 G191 G193 K194 T195 V196 Y376 F455 G155 G157 K158 T159 V160 Y340 F419
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
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:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0016020 membrane
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Cellular Component
External links
PDB RCSB:5fl7, PDBe:5fl7, PDBj:5fl7
PDBsum5fl7
PubMed27373333
UniProtQ6CFT7|ATPB_YARLI ATP synthase subunit beta, mitochondrial (Gene Name=ATP2)

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