Current Protein Identity：P04153
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1AY9 WILD-TYPE UMUD' FROM E. COLI Deposited 1997-11-15 | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count |
Chain A
32–139（108 aa）
Chain B
32–139（108 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 6；100MM CACODYLATE BUFFER PH 6.0
|
Resolution 3.00 Å R-free 0.287 |
| 1AY9 WILD-TYPE UMUD' FROM E. COLI Deposited 1997-11-15 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
32–139（108 aa）
Chain B
32–139（108 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 6；100MM CACODYLATE BUFFER PH 6.0
|
Resolution 3.00 Å R-free 0.287 |
| 1I4V SOLUTION STRUCTURE OF THE UMUD' HOMODIMER Deposited 2001-02-23 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
25–139（115 aa）
Chain B
25–139（115 aa）
|
Mutation：G25A Mutation：G25A | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 6；303 K；Ionic strength (raw mmCIF value) 150 mM NaCl；Pressure ambient
NMR sample composition
0.9 mM UmuD' U-15N; 150 mM NaCl, 10 mM phosphate, pH 6.0, 1mM DTT, 0.1 mM EDTA | 95% H2O/5% D2O
NMR sample composition
1.3 mM UmuD' U-15N,13C; 150 mM NaCl, 20 mM phosphate, pH 6.0, 1 mM DTT, 0.1 mM EDTA | 95% H2O/5% D2O
NMR sample composition
1.5 mM UmuD' unlabeled; 150 mM NaCl, 20 mM phosphate, pH 6.0, 1 mM DTT, 0.1 mM EDTA | 95% H20, 5% D2O
NMR sample composition
1.4 mM UmuD' unlabeled; 150 mM NaCl, 20 mM phosphate, pH 6.0, 1 mM DTT, 0.1 mM EDTA | 100% D2O
NMR sample composition
0.5 mM UmuD' U-10% 13C; 150 mM NaCl, 20 mM phosphate, pH 6.0, 1 mM DTT, 0.1 mM EDTA | 100% D2O
NMR sample composition
2.7 mM UmuD' U-100% 2H,15N and 2.7 mM unlabeled UmuD'; 150 mM NaCl, 20 mM phosphate, pH 6.0, 1 mM DTT, 0.1 mM EDTA | 95% H20, 5% D2O
|
Resolution not provided |
| 1UMU STRUCTURE DETERMINATION OF UMUD' BY MAD PHASING OF THE SELENOMETHIONYL PROTEIN Deposited 1996-03-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
25–139（115 aa）
Fragment：;UMUD', RESIDUES 25 - 139
;
Chain B
25–139（115 aa）
Fragment：;UMUD', RESIDUES 25 - 139
;
|
Mutation：DEL(1-24), M138T, M61 AND M110 SUBSTITUTED BY SELENOMETHIONINE Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：DEL(1-24), M138T, M61 AND M110 SUBSTITUTED BY SELENOMETHIONINE Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 5.8；THE CRYSTALS WERE GROWN FROM 600MM LISO4, 20MM MGCL2, 100MM CACODYLATE BUFFER PH 5.8, 5MM DTT AT 20C WITH A PROTEIN CONCENTRATION OF 12-15 MG/ML. THE CRYSTALS WERE FROZEN AT 100K IN PARATONE FOR DATA COLLECTION AT THE NSLS X4A BEAMLINE.
|
Resolution 2.50 Å R-free 0.303 |