Structure of PDB 7khr Chain C Binding Site BS01

Receptor Information
>7khr Chain C (length=600) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMA
TIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQ
TQSIYIPRGVNVSALSRDVKWDFTPCKNLRVGSHITGGDIYGIVNENSLI
KHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGIKEKFSMVQVWPVR
QVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQS
LSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALV
ANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREIS
GRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSP
PGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALD
EYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVA
KLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSD
NKITWSIIREHMGEILYKLSSMKFKDPVKDGEAKIKADYAQLLEDMQNAF
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain7khr Chain C Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7khr Molecular basis of V-ATPase inhibition by bafilomycin A1.
Resolution3.62 Å
Binding residue
(original residue number in PDB)		T257 R280 E283
Binding residue
(residue number reindexed from 1)		T245 R268 E271
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K256 E279 R280 K456
Catalytic site (residue number reindexed from 1) K244 E267 R268 K444
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006879 intracellular iron ion homeostasis
GO:0015986 proton motive force-driven ATP synthesis
GO:0036295 cellular response to increased oxygen levels
GO:0045851 pH reduction
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0000221 vacuolar proton-transporting V-type ATPase, V1 domain
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0030133 transport vesicle
GO:0030665 clathrin-coated vesicle membrane
GO:0031410 cytoplasmic vesicle
GO:0033180 proton-transporting V-type ATPase, V1 domain

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7khr, PDBe:7khr, PDBj:7khr
PDBsum7khr
PubMed33741963
UniProtP31404|VATA_BOVIN V-type proton ATPase catalytic subunit A (Gene Name=ATP6V1A)

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