Structure of PDB 5ik2 Chain K

Receptor sequence
>5ik2K (length=476) Species: 986075 (Caldalkalibacillus thermarum TA2.A1) [Search protein sequence]
EVVEVGTVIQVGDGIARVHGLEKVMAGELLEFENGVMGMAQNLEEDNVGV
VILGPYTEIREGTQVKRTGRIMEVPVGEALLGRVVNPLGQPLDGRGPIET
AEYRPIESPAPGVMDRKSVHEPLQTGIKAIDSMIPIGRGQRELIIGDRQT
GKTTIAIDTIINQKGQDVICIYVAIGQKQSTVAGVVETLRQHDALDYTIV
VTASASEPAPLLYLAPYAGCAMGEYFMYKGKHALVVYDDLSKQAAAYREL
SLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEKGGGSLTALPFIETQA
GDVSAYIPTNVISITDGQIFLESDLFYSGVRPAVNVGISVSRVGGAAQIK
AMKKVAGTLRLDLAQYRELQAFAQFGDKATQAKLNRGERTVEILKQDEHK
PMPVEEQVISIYAVTNGFMDDIPVEDVRRFEEELLSFMRANKDSLLDHIR
QTGELPDTKELDAAIEEFKKGFTPSA
3D structure
PDB5ik2 Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.
ChainK
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q200 K201 R365
Catalytic site (residue number reindexed from 1) K152 Q177 K178 R342
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 K Q172 G174 K175 T176 T177 F349 R354 E424 Q149 G151 K152 T153 T154 F326 R331 E398
BS02 ADP K V363 R365 V340 R342
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
GO:0046872 metal ion 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:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma 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:5ik2, PDBe:5ik2, PDBj:5ik2
PDBsum5ik2
PubMed27621435
UniProtF5LA74

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