[English] 日本語
![](img/lk-miru.gif)
- PDB-2dhf: CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE C... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2dhf | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND 5-DEAZOFOLATE | ||||||
![]() | DIHYDROFOLATE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / OXIDO-REDUCTASE | ||||||
Function / homology | ![]() regulation of removal of superoxide radicals / tetrahydrobiopterin biosynthetic process / Metabolism of folate and pterines / tetrahydrofolate metabolic process / sequence-specific mRNA binding / response to methotrexate / axon regeneration / folic acid binding / G1/S-Specific Transcription / dihydrofolate metabolic process ...regulation of removal of superoxide radicals / tetrahydrobiopterin biosynthetic process / Metabolism of folate and pterines / tetrahydrofolate metabolic process / sequence-specific mRNA binding / response to methotrexate / axon regeneration / folic acid binding / G1/S-Specific Transcription / dihydrofolate metabolic process / glycine biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process / NADPH binding / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / tetrahydrofolate biosynthetic process / mRNA regulatory element binding translation repressor activity / positive regulation of nitric-oxide synthase activity / one-carbon metabolic process / NADP binding / negative regulation of translation / mRNA binding / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Davies /II, J.F. / Kraut, J. | ||||||
![]() | ![]() Title: Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate. Authors: Davies 2nd., J.F. / Delcamp, T.J. / Prendergast, N.J. / Ashford, V.A. / Freisheim, J.H. / Kraut, J. #1: ![]() Title: Expression and Site-Directed Mutagenesis of Human Dihydrofolate Reductase Authors: Prendergast, N.J. / Delcamp, T.J. / Smith, P.L. / Freisheim, J.H. | ||||||
History |
| ||||||
Remark 650 | HELIX IN EACH CHAIN, RESIDUES ASP 21 - LEU 22 - PRO 23 - TRP 24 - PRO 25 - PRO 26 ARE IN LEFT- ...HELIX IN EACH CHAIN, RESIDUES ASP 21 - LEU 22 - PRO 23 - TRP 24 - PRO 25 - PRO 26 ARE IN LEFT-HANDED POLYPROLINE HELIX CONFORMATION. | ||||||
Remark 700 | SHEET THE FOLLOWING REMARKS APPLY TO EACH CHAIN. IN THE *HELIX*, *SHEET* AND *TURN* RECORDS BELOW, ...SHEET THE FOLLOWING REMARKS APPLY TO EACH CHAIN. IN THE *HELIX*, *SHEET* AND *TURN* RECORDS BELOW, AN *A* OR *B* HAS BEEN APPENDED TO THE NAMES USED IN THIS REMARK TO DISTINGUISH CHAINS. RESIDUE GLN 102 PARTICIPATES IN BOTH HELIX E AND EP. RESIDUES LYS 108 AND VAL 109 PARTICIPATE IN BOTH HELIX EP AND STRAND E. RESIDUE GLU 172 IS IN TIGHT-TURN 8 AND BETA STRAND G. RESIDUE ILE 175 IS IN TIGHT-TURN 8 AND BETA STRAND H. RESIDUES ASP 110 - MET 111 FORM A BETA-BULGE IN STRAND E. RESIDUES VAL 115 - GLY 116 FORM A BETA-BULGE IN STRAND E. TIGHT TURN 7 DISRUPTS STRAND G. THIS IS REPRESENTED ON THE SHEET RECORDS BELOW BY PRESENTING THE SHEET TWICE WITH STRAND 8 DIFFERENT. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 88.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 68.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 520.5 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 559.6 KB | Display | |
Data in XML | ![]() | 15.5 KB | Display | |
Data in CIF | ![]() | 21.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: RESIDUES PRO A 66 AND PRO B 66 ARE CIS PROLINES. 2: IN EACH CHAIN, THE PEPTIDE BOND LINKING GLY 116 TO GLY 117 IS IN THE CIS CONFORMATION. |
-
Components
#1: Protein | Mass: 21349.525 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 46.89 % | ||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 5.9 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 15545 / % possible obs: 95 % / Rmerge(I) obs: 0.05 |
---|
-
Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor obs: 0.194 / Highest resolution: 2.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|