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- PDB-2v7q: The structure of F1-ATPase inhibited by I1-60HIS, a monomeric for... -
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Basic information
Entry | Database: PDB / ID: 2v7q | ||||||
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Title | The structure of F1-ATPase inhibited by I1-60HIS, a monomeric form of the inhibitor protein, IF1. | ||||||
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![]() | HYDROLASE / ION TRANSPORT / MITOCHONDRION / TRANSIT PEPTIDE / INHIBITOR PROTEIN | ||||||
Function / homology | ![]() angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / negative regulation of hydrolase activity / proton-transporting ATP synthase complex / heme biosynthetic process / : ...angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / negative regulation of hydrolase activity / proton-transporting ATP synthase complex / heme biosynthetic process / : / : / Mitochondrial protein degradation / : / negative regulation of endothelial cell proliferation / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton transmembrane transport / aerobic respiration / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / erythrocyte differentiation / ADP binding / ATPase binding / protein homotetramerization / mitochondrial inner membrane / calmodulin binding / structural molecule activity / cell surface / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gledhill, J.R. / Montgomery, M.G. / Leslie, A.G.W. / Walker, J.E. | ||||||
![]() | ![]() Title: How the Regulatory Protein, If1, Inhibits F1- ATPase from Bovine Mitochondria. Authors: Gledhill, J.R. / Montgomery, M.G. / Leslie, A.G.W. / Walker, J.E. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 13-STRANDED BARREL THIS IS REPRESENTED BY A 14-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 679.2 KB | Display | ![]() |
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PDB format | ![]() | 552.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.8 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 92.7 KB | Display | |
Data in CIF | ![]() | 136.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ohhS ![]() 2uys S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-ATP SYNTHASE ... , 5 types, 9 molecules ABCDEFGHI
#1: Protein | Mass: 55332.219 Da / Num. of mol.: 3 / Fragment: RESIDUES 44-553 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: Q1JQC4, UniProt: P19483*PLUS, EC: 3.6.1.14 #2: Protein | Mass: 51757.836 Da / Num. of mol.: 3 / Fragment: RESIDUES 47-528 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Protein | | Mass: 30185.674 Da / Num. of mol.: 1 / Fragment: RESIDUES 26-297 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #4: Protein | | Mass: 15074.813 Da / Num. of mol.: 1 / Fragment: RESIDUES 23-168 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #5: Protein/peptide | | Mass: 5662.693 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Protein , 1 types, 1 molecules J
#6: Protein | Mass: 7462.098 Da / Num. of mol.: 1 / Fragment: RESIDUES 26-85 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 1951 molecules ![](data/chem/img/ATP.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
#7: Chemical | #8: Chemical | ChemComp-MG / #9: Chemical | #10: Chemical | ChemComp-PO4 / | #11: Water | ChemComp-HOH / | |
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-Details
Sequence details | I1-60HIS IS A TRUNCATED FRAGMENT OF THE BOVINE ATPASE INHIBITOR PROTEIN. RESIDUES 1-60 PLUS 6 C- ...I1-60HIS IS A TRUNCATED FRAGMENT OF THE BOVINE ATPASE INHIBITOR PROTEIN. RESIDUES 1-60 PLUS 6 C-TERMINAL HISTIDINES |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.21 % / Description: NONE |
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Crystal grow | pH: 8.2 / Details: pH 8.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→69.7 Å / Num. obs: 212416 / % possible obs: 99.2 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 9.1 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 2 / % possible all: 97.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1OHH Resolution: 2.1→37.19 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.916 / SU B: 10.233 / SU ML: 0.144 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.223 / ESU R Free: 0.193 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.41 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→37.19 Å
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Refine LS restraints |
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