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- PDB-2rsl: REFINEMENT OF GAMMA DELTA RESOLVASE REVEALS A STRIKINGLY FLEXIBLE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2rsl | |||||||||
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Title | REFINEMENT OF GAMMA DELTA RESOLVASE REVEALS A STRIKINGLY FLEXIBLE MOLECULE | |||||||||
![]() | GAMMA DELTA-RESOLVASE | |||||||||
![]() | SITE-SPECIFIC RECOMBINASE | |||||||||
Function / homology | ![]() | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Rice, P.A. / Steitz, T.A. | |||||||||
![]() | ![]() Title: Refinement of gamma delta resolvase reveals a strikingly flexible molecule. Authors: Rice, P.A. / Steitz, T.A. #1: ![]() Title: The Crystal Structure of the Catalytic Domain of the Site-Specific Recombination Enzyme Gamma Delta Resolvase at 2.7 Angstroms Resolution Authors: Sanderson, M.R. / Freemont, P.S. / Rice, P.A. / Goldman, A. / Hatfull, G.F. / Grindley, N.D.F. / Steitz, T.A. #2: ![]() Title: Protein-Protein Interactions Directing Resolvase Site-Specific Recombination: A Structure-Function Analysis Authors: Hughes, R.E. / Rice, P.A. / Steitz, T.A. / Grindley, N.D.F. #3: ![]() Title: Cooperativity Mutants of the Gamma Delta Resolvase Identify an Essential Interdimer Interaction Authors: Hughes, R.E. / Hatfull, G.F. / Rice, P. / Steitz, T.A. / Grindley, N.D.F. #4: ![]() Title: Preparation of Heavy-Atom Derivatives Using Site-Directed Mutagenesis. Introduction of Cysteine Residues Into Gamma Delta Resolvase Authors: Hatfull, G.F. / Sanderson, M.R. / Freemont, P.S. / Raccuia, P.R. / Grindley, N.D.F. / Steitz, T.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 94.7 KB | Display | ![]() |
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PDB format | ![]() | 74.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Details | THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW WERE CALCULATED BY A LEAST-SQUARES FITTING OF RESIDUES 1 - 36 AND 46 - 115 OF EACH MONOMER. THE TWIST OF THE CENTRAL BETA SHEET OF MONOMER A IS DIFFERENT THAN THAT OF THE OTHER TWO, SO THE CHOICE OF WHICH ATOMS TO SUPERIMPOSE IS SOMEWHAT ARBITRARY. THE TRANSFORMATION PRESENTED AS *MTRIX 1* BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED TO CHAIN A. THE TRANSFORMATION PRESENTED AS *MTRIX 2* BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN C WHEN APPLIED TO CHAIN A. THE TRANSFORMATION PRESENTED AS *MTRIX 3* BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN C WHEN APPLIED TO CHAIN B. |
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Components
#1: Protein | Mass: 15515.833 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ![]() #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.83 % | ||||||||||||||||||||||||
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Crystal grow![]() | *PLUS pH: 7.5 / Method: microdialysis | ||||||||||||||||||||||||
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 |
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Processing
Software |
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Refinement | Resolution: 2.3→8 Å / σ(F): 1 Details: THE TURN CONSISTING OF RESIDUES 38 - 44 IN CHAIN A AND THE C-TERMINUS OF EACH CHAIN (RESIDUES A 123 - A 140, B 121 - B 140, AND C 120 - C 140) ARE DISORDERED IN THE CRYSTAL. NO COORDINATES ...Details: THE TURN CONSISTING OF RESIDUES 38 - 44 IN CHAIN A AND THE C-TERMINUS OF EACH CHAIN (RESIDUES A 123 - A 140, B 121 - B 140, AND C 120 - C 140) ARE DISORDERED IN THE CRYSTAL. NO COORDINATES ARE INCLUDED IN THIS ENTRY FOR THESE RESIDUES.
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |