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- PDB-1nba: CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MEC... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1nba | ||||||
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Title | CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION | ||||||
![]() | N-CARBAMOYLSARCOSINE AMIDOHYDROLASE | ||||||
![]() | HYDROLASE(IN LINEAR AMIDES) | ||||||
Function / homology | ![]() N-carbamoylsarcosine amidase / N-carbamoylsarcosine amidase activity / creatinine catabolic process Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Romao, M.J. / Turk, D. / Gomis-Ruth, F.-Z. / Huber, R. / Schumacher, G. / Mollering, H. / Russmann, L. | ||||||
![]() | ![]() Title: Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution. Authors: Romao, M.J. / Turk, D. / Gomis-Ruth, F.X. / Huber, R. / Schumacher, G. / Mollering, H. / Russmann, L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 208.4 KB | Display | ![]() |
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PDB format | ![]() | 168.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 395 KB | Display | ![]() |
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Full document | ![]() | 411.6 KB | Display | |
Data in XML | ![]() | 21.4 KB | Display | |
Data in CIF | ![]() | 34.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: ALA A 172 - THR A 173 OMEGA =352.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: ALA B 172 - THR B 173 OMEGA =354.44 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: ALA C 172 - THR C 173 OMEGA =352.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: ALA D 172 - THR D 173 OMEGA =355.08 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 29084.311 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.46 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5 / Method: vapor diffusion / Details: drop-0.002ml, reservoir-0.003ml | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 9999 Å / Num. obs: 62120 / % possible obs: 73.2 % / Num. measured all: 147634 / Rmerge(I) obs: 0.111 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.1 Å / % possible obs: 40.8 % |
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Processing
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Refinement | Rfactor Rwork: 0.186 / Rfactor obs: 0.186 / Highest resolution: 2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / Num. reflection obs: 56641 / Rfactor obs: 0.186 / Rfactor Rwork: 0.186 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.7 |