Current Protein Identity:P17571
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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 |
|---|---|---|---|---|---|---|---|
| 1CNE STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN Deposited 1995-02-01 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
352–621(270 aa)
|
Not recorded | FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 3.00 Å |
| 1CNF STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN Deposited 1995-02-01 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
352–621(270 aa)
|
Not recorded | FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.70 Å R-free 0.272 |
| 2CND STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN Deposited 1995-02-01 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
352–621(270 aa)
|
Not recorded | FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.50 Å R-free 0.223 |