[English] 日本語
![](img/lk-miru.gif)
- PDB-1iuu: P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 9.4 -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1iuu | ||||||
---|---|---|---|---|---|---|---|
Title | P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 9.4 | ||||||
![]() | P-HYDROXYBENZOATE HYDROXYLASE | ||||||
![]() | ![]() | ||||||
Function / homology | ![]() 4-hydroxybenzoate 3-monooxygenase (NADPH) activity / ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Gatti, D.L. / Entsch, B. / Ballou, D.P. / Ludwig, M.L. | ||||||
![]() | ![]() Title: pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis. Authors: Gatti, D.L. / Entsch, B. / Ballou, D.P. / Ludwig, M.L. #1: ![]() Title: Crystal Structures of Wild-Type P-Hydroxybenzoate Hydroxylase Complexed with 4-Aminobenzoate, 2,4-Dihydrobenzoate and 2-Hydroxy-4-Aminobenzoate and of the Tyr222Ala Mutant Complexed with 2- ...Title: Crystal Structures of Wild-Type P-Hydroxybenzoate Hydroxylase Complexed with 4-Aminobenzoate, 2,4-Dihydrobenzoate and 2-Hydroxy-4-Aminobenzoate and of the Tyr222Ala Mutant Complexed with 2-Hydroxy-4-Aminobenzoate.Evidence for a Proton Channel and a New Binding Mode of the Flavin Ring Authors: Schreuder, H.A. / Mattevi, A. / Obmolova, G. / Kalk, K.H. / Hol, W.G.J. #2: ![]() Title: Crystal Structures of Mutant Pseudomonas Aeruginosa P-Hydroxybenzoate Hydroxylases:The Tyr201Phe, Tyr385Phe and Asn300Asp Variants Authors: Lah, M.S. / Palfey, B.A. / Schreuder, H.A. / Ludwig, M.L. #3: ![]() Title: Catalytic Function of Tyrosine Residues in Para-Hydroxybenzoate Hydroxylase as Determined by the Study of Site-Directed Mutants Authors: Entsch, B. / Palfey, B.A. / Ballou, D.P. / Massey, V. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 98 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 74 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO 275 |
-
Components
#1: Protein | Mass: 44382.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: PH 9.4 STRUCTURE / Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P20586, ![]() |
---|---|
#2: Chemical | ChemComp-FAD / ![]() |
#3: Chemical | ChemComp-PAB / ![]() |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.84 % | ||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow![]() | pH: 9.4 / Details: pH 9.4 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4-23 ℃ / pH: 7.4 / Method: interface diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 295 K |
---|---|
Diffraction source | Wavelength: 1.5418 Å |
Detector | Type: SDMS / Detector: AREA DETECTOR / Details: 0.5 MM COLLIMATOR |
Radiation | Monochromator: GRAPHITE / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2→15 Å / % possible obs: 98.73 % / Redundancy: 5.96 % / Rmerge(I) obs: 0.112 / Net I/σ(I): 8.91 |
Reflection shell | Resolution: 2→2.15 Å / Rmerge(I) obs: 0.336 / Mean I/σ(I) obs: 2.08 / % possible all: 95.34 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 15 Å / Num. obs: 31276 / % possible obs: 98.73 % / Redundancy: 8.25 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2→15 Å / σ(F): 0 Details: THE HYDROGEN BOND DISTANCE CUTOFF USED FOR THE TURNS IS 3.5 ANGSTROMS. THE CA(X) TO CA(X+4) DISTANCE IS LESS THAN 6.0 ANGSTROMS. THE ANGLES ARE FROM ROBSON AND GARNIER, (1986), 'INTRODUCTION ...Details: THE HYDROGEN BOND DISTANCE CUTOFF USED FOR THE TURNS IS 3.5 ANGSTROMS. THE CA(X) TO CA(X+4) DISTANCE IS LESS THAN 6.0 ANGSTROMS. THE ANGLES ARE FROM ROBSON AND GARNIER, (1986), 'INTRODUCTION TO PROTEINS AND PROTEIN ENGINEERING', ELSEVIER, AMSTERDAM. TYPE PHI2 PSI2 PHI3 PSI3 I -75(+-65) -30(+-40) -90(+-40) -15 TO 40 II -60(+-40) 120(+-40) 90(+-40) 0(+-40) III -75(+-65) -30(+-40) -60(+-40) -15 TO -70 I(PRIME) 75(+-65) 30(+-40) 90(+-40) -40 TO 15 II(PRIME) 60(+-40) -120(+-40) -90(+-40) 0(+-40) III(PRIME) 75(+-65) 30(+-40) 60(+-40) 15 TO 70 MODIFIED CYSTEINE WITH ADDITIONAL ELECTRON DENSITY NEAR THE SULFUR AT X=5.26, Y=107.89, Z=71.02 - CYS 116. THE TYPE OF CHEMICAL MODIFICATION CANNOT BE UNAMBIGUOUSLY DETERMINED FROM THE ELECTRON DENSITY THE SIDE CHAINS OF RESIDUES 135, 136, 146, 392, 393, 394 ARE NOT ORDERED. THE MODEL IS DERIVED FROM A COMBINATION OF FIT TO RESIDUAL DENSITY AND ENERGY MINIMIZATION.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→15 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|