+
Open data
-
Basic information
Entry | Database: PDB / ID: 1c21 | ||||||
---|---|---|---|---|---|---|---|
Title | E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE COMPLEX | ||||||
![]() | METHIONINE AMINOPEPTIDASE | ||||||
![]() | HYDROLASE / PRODUCT COMPLEX | ||||||
Function / homology | ![]() : / initiator methionyl aminopeptidase activity / methionyl aminopeptidase / metalloaminopeptidase activity / ferrous iron binding / proteolysis / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Lowther, W.T. / Zhang, Y. / Sampson, P.B. / Honek, J.F. / Matthews, B.W. | ||||||
![]() | ![]() Title: Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues. Authors: Lowther, W.T. / Zhang, Y. / Sampson, P.B. / Honek, J.F. / Matthews, B.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 66.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 47.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 439.7 KB | Display | |
Data in XML | ![]() | 13.1 KB | Display | |
Data in CIF | ![]() | 18.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 29210.580 Da / Num. of mol.: 1 / Fragment: METHIONINE / Mutation: R175Q Source method: isolated from a genetically manipulated source Details: METHIONINE COMPLEX / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P07906, UniProt: P0AE18*PLUS, methionyl aminopeptidase | ||||||||
---|---|---|---|---|---|---|---|---|---|
#2: Chemical | #3: Chemical | ChemComp-NA / | #4: Chemical | ChemComp-MET / | #5: Water | ChemComp-HOH / | Sequence details | THERE ARE FOUR ADDITIONAL RESIDUES ON THE C-TERMINUS LEFT OVER FROM A THROMBIN DIGEST OF THE HIS- ...THERE ARE FOUR ADDITIONAL | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.58 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: K2SO4, NaCl, methionine, N-octanoyl sucrose, PEG 4000, HEPES, CoCl2, VAPOR DIFFUSION, SITTING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 298 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Apr 23, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→24.8 Å / Num. all: 21097 / Num. obs: 85232 / % possible obs: 95.1 % / Redundancy: 4 % / Biso Wilson estimate: 19.4 Å2 / Rmerge(I) obs: 0.045 / Net I/σ(I): 35.2 |
Reflection shell | Resolution: 1.8→1.86 Å / Rmerge(I) obs: 0.256 / Mean I/σ(I) obs: 4.4 / % possible all: 90.2 |
Reflection | *PLUS Num. obs: 21097 / Num. measured all: 85232 |
Reflection shell | *PLUS % possible obs: 90.2 % |
-
Processing
Software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.8→24.8 Å / Stereochemistry target values: TNT /
| |||||||||||||||
Solvent computation | Solvent model: TNT / Bsol: 204.6 Å2 / ksol: 0.834 e/Å3 | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→24.8 Å
| |||||||||||||||
Refine LS restraints |
| |||||||||||||||
Software | *PLUS Name: TNT / Classification: refinement | |||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / Rfactor all: 0.163 / Num. reflection obs: 21097 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
|