Structure of PDB 3oaa Chain Z

Receptor sequence
>3oaaZ (length=486) Species: 536056 (Escherichia coli DH1) [Search protein sequence]
HNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVV
MGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDG
FSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGK
TALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVV
ATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISL
LLRRPPGREAFPGDVFYLHSRLLERAARVNAEYVEAFTKGEVKGKTGSLT
ALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVS
RVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQ
KVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYV
DRDHAPLMQEINQTGGYNDEIEGKLKGILDSFKATQ
3D structure
PDB3oaa Structural basis for inhibition of bacterial ATP synthase by subunit epsilon of the rotor stalk
ChainZ
Resolution3.26 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 R376
Catalytic site (residue number reindexed from 1) K150 Q175 K176 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 ANP Z Q172 G174 K175 T176 A177 F360 R365 Q433 K434 Q435 Q147 G149 K150 T151 A152 F335 R340 Q408 K409 Q410
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
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:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma 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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3oaa, PDBe:3oaa, PDBj:3oaa
PDBsum3oaa
PubMed
UniProtP0ABB0|ATPA_ECOLI ATP synthase subunit alpha (Gene Name=atpA)

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