Structure of PDB 5knc Chain C

Receptor sequence
>5kncC (length=586) Species: 768486 (Enterococcus hirae ATCC 9790) [Search protein sequence]
MQIGKIIKVSGPLVMAENMSEASIQDMCLVGDLGVIGEIIEMRQDVASIQ
VYEETSGIGPGEPVRSTGEALSVELGPGIISQMFDGIQRPLDTFMEVTQS
NFLGRGVQLPALDHEKQWWFEATIEEGTEVSAGDIIGYVDETKIIQHKIM
VPNGIKGTVQKIESGSFTIDDPICVIETEQGLKELTMMQKWPVRRGRPIK
QKLNPDVPMITGQRVIDTFFPVTKGGAAAVPGPFGAGKTVVQHQIAKWSD
VDLVVYVGCGERGNEMTDVVNEFPELIDPNTGESLMERTVLIANTSNMPV
AAREASIYTGITIAEYFRDMGYDVAIMADSTSRWAEALREMSGRLEEMPG
DEGYPAYLGSRLAEYYERSGRVIALGSDQREGSITAISAVSPSGGDISEP
VTQNTLRVVKVFWGLDSSLAQKRHFPSINWIQSYSLYSTEVGRYMDQILQ
QDWSDMVTEGMRILQEEEQLNEIVRLVGIDSLSDNDRLTLEVAKSIREDY
LQQNAFDDVDTFTSREKQFNMLKVILTFGKEARKALSLGAYFNEIMEGTV
AVRERISRSKYIPEEELAKISSINEEIKETIQLIVS
3D structure
PDB5knc Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor
ChainC
Resolution3.015 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K238 E261 R262 L436
Catalytic site (residue number reindexed from 1) K238 E261 R262 L436
Enzyme Commision number 7.2.2.1: Na(+)-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 C G235 A236 G237 K238 T239 V240 F425 A505 F506 G235 A236 G237 K238 T239 V240 F425 A505 F506
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0046932 sodium-transporting ATP synthase activity, rotational mechanism
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
GO:0046962 sodium-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006814 sodium ion transport
GO:0035725 sodium ion transmembrane transport
GO:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0045259 proton-transporting ATP synthase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5knc, PDBe:5knc, PDBj:5knc
PDBsum5knc
PubMed27807367
UniProtQ08636|NTPA_ENTHA V-type sodium ATPase catalytic subunit A (Gene Name=ntpA)

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