Structure of PDB 6ly8 Chain A

Receptor sequence

>6ly8A (length=577) Species: 300852 (Thermus thermophilus HB8)

MIQGVIQKIAGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQ
VYEDTSGLKVGEPVVSTGLPLAVELGPGMLNGIYDGIQRPLERIREKTGI
YITRGVVVHALDREKKWAWTPMVKPGDEVRGGMVLGTVPEFGFTHKILVP
PDVRGRVKEVKPAGEYTVEEPVVVLEDGTELKMYHTWPVRRARPVQRKLD
PNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVV
VYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAARE
ASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGY
PPYLAARLAAFYERAGKVITLGGEEGAVTIVGAVSPPGGDMSEPVTQSTL
RIVGAFWRLDASLAFRRHFPAINWNGSYSLFTSALDPWYRENVAEDYPEL
RDAISELLQREAGLQEIVQLVGPDALQDAERLVIEVGRIIREDFLQQNAY
HEVDAYCSMKKAYGIMKMILAFYKEAEAAIKRGVSIDEILQLPVLERIGR
ARYVSEEEFPAYFEEAMKEIQGAFKAL

3D structure

• PDB: 6ly8 Mechanical inhibition of isolated V o from V/A-ATPase for proton conductance.
• Chain: A
• Resolution: 3.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K234 E257 R258 L430
• Catalytic site (residue number reindexed from 1): K234 E257 R258 L430
• 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	A	G231 S232 G233 K234 T235 V236 F419	G231 S232 G233 K234 T235 V236 F419

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• GO:0005524 ATP 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: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

External links

• PDB: RCSB:6ly8, PDBe:6ly8, PDBj:6ly8
• PDBsum: 6ly8
• PubMed: 32639230
• UniProt: Q56403|VATA_THET8 V-type ATP synthase alpha chain (Gene Name=atpA)