Data selection

Experimental method
Exclude entries with
Mutations (vs. UniProt)
Number of data: 3898 Dataset: (exptl_method: X-ray) and (resolution_limit=2.0)
pdb_00003fvb Crystal structure of ferritin (bacterioferritin) from Brucella melitensis
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.806 Å
Deposition date 2009-01-15
pdb_00003fwf Ferric camphor bound cytochrome P450cam containing a Selenocysteine as the 5th heme ligand, monoclinic crystal form
Experimental method X-RAY DIFFRACTION
Structural data unavailable
Non-standard amino acids Included
Missing residues/ Structural gap None / None
Resolution 1.83 Å
Deposition date 2009-01-18
pdb_00003fwg Ferric camphor bound Cytochrome P450cam, Arg365Leu, Glu366Gln, monoclinic crystal form
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.55 Å
Deposition date 2009-01-18
pdb_00003fwj Ferric camphor bound Cytochrome P450cam containing a selenocysteine as the 5th heme ligand, orthorombic crystal form
Experimental method X-RAY DIFFRACTION
Structural data unavailable
Non-standard amino acids Included
Missing residues/ Structural gap None / None
Resolution 1.9 Å
Deposition date 2009-01-18
pdb_00003g1q Crystal structure of sterol 14-alpha demethylase (CYP51) from Trypanosoma brucei in ligand free state
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.89 Å
Deposition date 2009-01-30
pdb_00003g46 Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chloroform bound to the XE4 cavity
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 0.91 Å
Deposition date 2009-02-03
pdb_00003g4q Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chloroform bound to the XE4 cavity
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.6 Å
Deposition date 2009-02-04
pdb_00003g4r Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to HEME and dichloroethane bound to the XE4 cavity
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.6 Å
Deposition date 2009-02-04
pdb_00003g4w Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chlorobenzene bound to the XE4 cavity
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.9 Å
Deposition date 2009-02-04
pdb_00003g4y Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chloromethyl benzene bound to the XE4 cavity
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.7 Å
Deposition date 2009-02-04
pdb_00003g52 Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chloroethyl benzene bound to the XE4 cavity
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.65 Å
Deposition date 2009-02-04
pdb_00003g53 Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chloropropyl benzene bound to the XE4 cavity
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.64 Å
Deposition date 2009-02-04
pdb_00003g5f Crystallographic analysis of cytochrome P450 cyp121
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.4 Å
Deposition date 2009-02-05
pdb_00003g5h Crystallographic analysis of cytochrome P450 cyp121
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.4 Å
Deposition date 2009-02-05
pdb_00003gas Crystal Structure of Helicobacter pylori Heme Oxygenase Hugz in Complex with Heme
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids Included
Missing residues/ Structural gap None / None
Resolution 1.8 Å
Deposition date 2009-02-18
pdb_00003gdj Crystal structure determination of camel(Camelus dromedarius)hemoglobin at 2 angstrom resolution
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 2 Å
Deposition date 2009-02-24
pdb_00003gk9 Crystal structure of murine Ngb under Xe pressure
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.8 Å
Deposition date 2009-03-10
pdb_00003gkt Crystal structure of murine neuroglobin under Kr pressure
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.86 Å
Deposition date 2009-03-11
pdb_00003gkv X-ray structure of an intermediate along the oxidation pathway of Trematomus bernacchii hemoglobin
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.4 Å
Deposition date 2009-03-11
pdb_00003gm6 Structure of the Thioalkalivibrio nitratireducens cytochrome c nitrite reductase in complex with phosphate
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap Exists / None
Resolution 1.8 Å
Deposition date 2009-03-13