Structure of PDB 2f43 Chain B Binding Site BS02

Receptor Information
>2f43 Chain B (length=471) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SAAPKAGTATGQIVAVIGAVVDVQFDEGLPPILNALEVQGRESRLVLEVA
QHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGE
PIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGG
KIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEM
IESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQD
VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK
KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDP
LDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEER
ARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGDYDHLPEQA
FYMVGPIEEAVAKADKLAEEH
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 chain2f43 Chain B Residue 605 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2f43 Mitochondrial ATP synthase: Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		T163 E188
Binding residue
(residue number reindexed from 1)		T163 E188
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K162 E188 R189 R356
Catalytic site (residue number reindexed from 1) K162 E188 R189 R356
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0030228 lipoprotein particle receptor activity
GO:0042288 MHC class I protein binding
GO:0043531 ADP binding
GO:0043532 angiostatin binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0001525 angiogenesis
GO:0001889 liver development
GO:0006629 lipid metabolic process
GO:0006754 ATP biosynthetic process
GO:0006898 receptor-mediated endocytosis
GO:0006933 negative regulation of cell adhesion involved in substrate-bound cell migration
GO:0009631 cold acclimation
GO:0010042 response to manganese ion
GO:0015986 proton motive force-driven ATP synthesis
GO:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0043536 positive regulation of blood vessel endothelial cell migration
GO:0046034 ATP metabolic process
GO:0051453 regulation of intracellular pH
GO:0098761 cellular response to interleukin-7
GO:1901653 cellular response to peptide
GO:1902600 proton transmembrane transport
GO:1904643 response to curcumin
GO:1905242 response to 3,3',5-triiodo-L-thyronine
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0016020 membrane
GO:0031966 mitochondrial membrane
GO:0042645 mitochondrial nucleoid
GO:0045121 membrane raft
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:2f43, PDBe:2f43, PDBj:2f43
PDBsum2f43
PubMed16531409
UniProtP10719|ATPB_RAT ATP synthase subunit beta, mitochondrial (Gene Name=Atp5f1b)

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