Structure of PDB 2hld Chain X Binding Site BS01

Receptor Information
>2hld Chain X (length=469) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGE
NTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDER
GPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLF
GGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGV
INLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFID
NIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTS
VQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSR
LLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVER
ARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHA
FYMVGGIEDVVAKAEKLAA
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 chain2hld Chain X Residue 700 [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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PDB2hld Novel features of the rotary catalytic mechanism revealed in the structure of yeast F(1) ATPase.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		T164 E189 E193
Binding residue
(residue number reindexed from 1)		T158 E183 E187
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K163 E189 R190 R356
Catalytic site (residue number reindexed from 1) K157 E183 R184 R350
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005758 mitochondrial intermembrane space
GO:0005829 cytosol
GO:0016020 membrane
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)
GO:0045267 proton-transporting ATP synthase, catalytic core

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2hld, PDBe:2hld, PDBj:2hld
PDBsum2hld
PubMed17082766
UniProtP00830|ATPB_YEAST ATP synthase subunit beta, mitochondrial (Gene Name=ATP2)

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