Structure of PDB 6j5k Chain BD Binding Site BS02

Receptor Information
>6j5k Chain BD (length=469) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTV
RTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPI
KTKQFAAIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGA
GVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL
KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNI
FRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQ
AIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIM
DPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR
KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFY
MVGPIEEAVAKADKLAEEH
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 chain6j5k Chain BD Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6j5k Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.
Resolution6.2 Å
Binding residue
(original residue number in PDB)		T165 E194
Binding residue
(residue number reindexed from 1)		T155 E184
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K164 E190 R191 R358
Catalytic site (residue number reindexed from 1) K154 E180 R181 R348
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
Biological Process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6j5k, PDBe:6j5k, PDBj:6j5k
PDBsum6j5k
PubMed31197009
UniProtK7GLT8

[Back to BioLiP]