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Open data
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Basic information
Entry | Database: PDB / ID: 2rkm | ||||||
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Title | STRUCTURE OF OPPA COMPLEXED WITH LYS-LYS | ||||||
![]() | OLIGO-PEPTIDE BINDING PROTEIN | ||||||
![]() | PEPTIDE BINDING PROTEIN / PEPTIDE TRANSPORT / COMPLEX (BINDING PROTEIN-DIPEPTIDE) | ||||||
Function / homology | ![]() peptide transmembrane transporter activity / peptide transport / ATP-binding cassette (ABC) transporter complex / protein transport / outer membrane-bounded periplasmic space Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Sleigh, S.H. / Tame, J.R.H. / Wilkinson, A.J. | ||||||
![]() | ![]() Title: Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine. Authors: Sleigh, S.H. / Tame, J.R. / Dodson, E.J. / Wilkinson, A.J. #1: ![]() Title: The Role of Water in Sequence-Independent Ligand Binding by an Oligopeptide Transporter Protein Authors: Tame, J.R. / Sleigh, S.H. / Wilkinson, A.J. / Ladbury, J.E. #2: ![]() Title: Structure Determination of Oppa at 2.3 Angstroms Resolution Using Multiple Wavelength Anomalous Methods Authors: Glover, I.D. / Denny, R. / Nguti, N.D. / Mcsweeney, S. / Thompson, A. / Dodson, E. / Wilkinson, A.J. / Tame, J.R.H. #3: ![]() Title: The Crystal Structures of the Oligopeptide-Binding Protein Oppa Complexed with Tripeptide and Tetrapeptide Ligands Authors: Tame, J.R. / Dodson, E.J. / Murshudov, G. / Higgins, C.F. / Wilkinson, A.J. #4: ![]() Title: The Structural Basis of Sequence-Independent Peptide Binding by Oppa Protein Authors: Tame, J.R. / Murshudov, G.N. / Dodson, E.J. / Neil, T.K. / Dodson, G.G. / Higgins, C.F. / Wilkinson, A.J. | ||||||
History |
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Remark 700 | SHEET THE HELIX AND SHEET RECORDS PRESENTED HERE DIFFER FROM THE LIST WHICH THE PDB HAS GENERATED ...SHEET THE HELIX AND SHEET RECORDS PRESENTED HERE DIFFER FROM THE LIST WHICH THE PDB HAS GENERATED USING DSSP WHICH APPEAR ON ACTUAL HELIX AND SHEET RECORDS FURTHER DOWN IN THE ENTRY. BECAUSE OF LINE LENGTH LIMITATIONS THE FORMAT OF THE SHEET INFORMATION PRESENTED IN THIS REMARK HAS BEEN MODIFIED. HELIX 1 1 VAL A 34 LEU A 43 1 HELIX 2 2 HIS A 91 ALA A 101 1 HELIX 3 3 TYR A 112 GLY A 116 1 HELIX 4 4 ILE A 121 ALA A 126 1 HELIX 5 5 LYS A 169 PHE A 175 1 HELIX 6 6 GLU A 229 SER A 238 1 HELIX 7 7 ILE A 250 GLU A 259 1 HELIX 8 8 VAL A 287 ALA A 296 1 HELIX 9 9 ARG A 299 LYS A 305 1 HELIX 10 10 GLN A 337 ALA A 351 1 HELIX 11 11 ASP A 369 LEU A 386 1 HELIX 12 12 TRP A 397 GLN A 406 1 HELIX 13 13 THR A 424 LEU A 427 1 HELIX 14 14 PRO A 444 LYS A 455 1 HELIX 15 15 ASP A 459 ASP A 476 1 SH 1 A 7 VAL A 264 PRO A 268 0 SH 2 A 7 VAL A 486 LEU A 490 -1 N ARG A 489 O ARG A 265 SH 3 A 7 ASP A 242 TYR A 245 -1 N THR A 244 O LEU A 490 SH 4 A 7 THR A 14 ASN A 18 1 N ASN A 18 O MET A 243 SH 5 A 7 GLN A 220 LEU A 224 1 N GLN A 220 O LEU A 15 SH 6 A 7 ARG A 201 ARG A 206 -1 N LEU A 204 O VAL A 221 SH 7 A 7 TYR A 191 VAL A 197 -1 N VAL A 197 O ARG A 201 SH 1 B 4 ALA A 61 LYS A 67 0 SH 2 B 4 VAL A 71 LEU A 76 -1 N HIS A 75 O GLU A 62 SH 3 B 4 THR A 143 THR A 147 -1 N VAL A 146 O TRP A 72 SH 4 B 4 VAL A 136 ASP A 140 -1 N ASP A 140 O THR A 143 SH 1 C 5 ASN A 389 GLN A 395 0 SH 2 C 5 THR A 360 ASN A 366 1 O TYR A 365 N GLN A 395 SH 3 C 5 VAL A 411 CYS A 417 1 O VAL A 411 N LEU A 364 SH 4 C 5 CYS A 271 ILE A 277 -1 N GLU A 276 O ALA A 412 SH 5 C 5 ILE A 479 TYR A 484 -1 N TYR A 483 O TYR A 273 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 126.3 KB | Display | ![]() |
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PDB format | ![]() | 101.2 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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
#1: Protein | Mass: 58878.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: THE OLIGOPEPTIDE BINDING PROTEIN OPPA IS SYNTHESISED AS A 542 AMINO ACID PRE-PROTEIN. THE 25 AMINO ACID SIGNAL PEPTIDE IS CLEAVED FROM THE N-TERMINUS TO GIVE A 517 RESIDUE MATURE PROTEIN IN ...Details: THE OLIGOPEPTIDE BINDING PROTEIN OPPA IS SYNTHESISED AS A 542 AMINO ACID PRE-PROTEIN. THE 25 AMINO ACID SIGNAL PEPTIDE IS CLEAVED FROM THE N-TERMINUS TO GIVE A 517 RESIDUE MATURE PROTEIN IN THE PERIPLASMIC SPACE. ALL 517 RESIDUES ARE VISIBLE IN THE ELECTRON DENSITY MAP. Source: (natural) ![]() | ||||||
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#2: Chemical | #3: Chemical | ChemComp-IUM / #4: Water | ChemComp-HOH / | Nonpolymer details | THE RESIDUES 2001 AND 2002 REPRESENT A DIPEPTIDE (LYS-LYS) BOUND TO PERIPLASMIC OLIGOPEPTIDE- ...THE RESIDUES 2001 AND 2002 REPRESENT A DIPEPTIDE (LYS-LYS) BOUND TO PERIPLASMI | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.2 % | |||||||||||||||||||||||||
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Crystal grow | pH: 5.5 Details: 7% PEG 4K, 50MM SODIUM ACETATE PH5.5, 1MM URANYL ACETATE AND 30MG/ML OPPA | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 4, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. obs: 57099 / % possible obs: 92.9 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 7.6 |
Reflection shell | Resolution: 1.8→1.89 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.219 / Mean I/σ(I) obs: 3.4 / % possible all: 92.9 |
Reflection | *PLUS Num. measured all: 379533 |
Reflection shell | *PLUS % possible obs: 98.9 % |
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Processing
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Refinement | Resolution: 1.8→20 Å / Cross valid method: FREE R / σ(F): 0 Details: THE EIGHT URANIUM IONS HAVE ASSOCIATED OXYGEN ATOMS IN THE MODEL. THE GEOMETRY OF THESE URANYL IONS HAS NOT BEEN RESTRAINED OR MANUALLY MODIFIED. THE (O-U-O)2+ ION SHOULD BE LINEAR WITH AN O- ...Details: THE EIGHT URANIUM IONS HAVE ASSOCIATED OXYGEN ATOMS IN THE MODEL. THE GEOMETRY OF THESE URANYL IONS HAS NOT BEEN RESTRAINED OR MANUALLY MODIFIED. THE (O-U-O)2+ ION SHOULD BE LINEAR WITH AN O-U DISTANCE OF APPROXIMATELY 1.8 ANGSTROMS. SOLVENT STRUCTURE AROUND THE URANYL IONS IS TENTATIVE. URANIUM 8 IS PARTIALLY OCCUPIED AND THE DENSITY AROUND IT IS NOT CONCLUSIVE; HENCE THE SECOND OXYGEN IS MISSING. THE EIGHT URANIUM IONS HAVE ASSOCIATED OXYGEN ATOMS IN THE MODEL. THE GEOMETRY OF THESE URANYL IONS HAS NOT BEEN RESTRAINED OR MANUALLY MODIFIED. THE (O-U-O)2+ ION SHOULD BE LINEAR WITH AN O-U DISTANCE OF APPROXIMATELY 1.8 ANGSTROMS.
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Displacement parameters | Biso mean: 16.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.167 / Rfactor Rfree: 0.202 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |