Data selection

Experimental method
Exclude entries with
Mutations (vs. UniProt)
Number of data: 7660 Dataset: all data
pdb_00003pi1 Crystallographic Structure of HbII-oxy from Lucina pectinata at pH 9.0
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 2.002 Å
Deposition date 2010-11-05
pdb_00003pi2 Crystallographic Structure of HbII-oxy from Lucina pectinata at pH 8.0
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.85 Å
Deposition date 2010-11-05
pdb_00003pi3 Crystallographic Structure of HbII-oxy from Lucina pectinata at pH 5.0
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.95 Å
Deposition date 2010-11-05
pdb_00003pi4 Crystallographic Structure of HbII-oxy from Lucina pectinata at pH 4.0
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 3.17 Å
Deposition date 2010-11-05
pdb_00003pi8 Site-specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry as a Viable Alternative to PEGylation
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 2.2 Å
Deposition date 2010-11-05
pdb_00003pi9 Site-specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry as a Viable Alternative to PEGylation
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 2.9 Å
Deposition date 2010-11-05
pdb_00003pia Site-specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry as a Viable Alternative to PEGylation
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 2.1 Å
Deposition date 2010-11-05
pdb_00003pm0 Structural Characterization of the Complex between Alpha-Naphthoflavone and Human Cytochrome P450 1B1 (CYP1B1)
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap Exists / Exists
Resolution 2.7 Å
Deposition date 2010-11-15
pdb_00003pmq Crystal structure of the outer membrane decaheme cytochrome MtrF
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 3.2 Å
Deposition date 2010-11-17
pdb_00003pne Structure of rat neuronal nitric oxide synthase heme domain in complex with 6-(((3R,4R)-4-(2-((2,2-Difluoro-2-(3-chlorophenyl)ethyl)amino)ethoxy)pyrrolidin-3-yl)methyl)-4-methylpyridin-2-amine
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap Exists / Exists
Resolution 1.97 Å
Deposition date 2010-11-18
pdb_00003pnf Structure of rat neuronal nitric oxide synthase heme domain in complex with 6-(((3R,4R)-4-(2-((2,2-Difluoro-2-(2-chlorophenyl)ethyl)amino)ethoxy)pyrrolidin-3-yl)methyl)-4-methylpyridin-2-amine
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap Exists / Exists
Resolution 1.94 Å
Deposition date 2010-11-18
pdb_00003png Structure of rat neuronal nitric oxide synthase heme domain in complex with 6-(((3R,4R)-4-(2-((2-fluoro-2-(3-fluorophenyl)ethyl)amino)ethoxy)pyrrolidin-3-yl)methyl)-4-methylpyridin-2-amine
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap Exists / Exists
Resolution 1.88 Å
Deposition date 2010-11-18
pdb_00003pnh Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in complex with 6-(((3R,4R)-4-(2-((2-FLUORO-2-(3-FLUOROPHENYL) ETHYL)AMINO)ETHOXY)PYRROLIDIN-3-YL)METHYL)-4-METHYLPYRIDIN-2-AMINE
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap Exists / Exists
Resolution 1.93 Å
Deposition date 2010-11-18
pdb_00003prc PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS (QB-DEPLETED)
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids Included
Missing residues/ Structural gap None / None
Resolution 2.4 Å
Deposition date 1997-07-29
pdb_00003psx Crystal structure of the KT2 mutant of cytochrome P450 BM3
Experimental method X-RAY DIFFRACTION
Structural data unavailable
Non-standard amino acids None
Missing residues/ Structural gap Exists / Exists
Resolution 1.9 Å
Deposition date 2010-12-02
pdb_00003pt7 Structure of HbII-III-Oxy from Lucina pectinata at pH 5.0
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 2.15 Å
Deposition date 2010-12-02
pdb_00003pt8 Structure of HbII-III-CN from Lucina pectinata at pH 5.0
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids None
Missing residues/ Structural gap None / None
Resolution 1.762 Å
Deposition date 2010-12-02
pdb_00003pxs Crystal Structure of Diferrous MauG in Complex with Pre-Methylamine Dehydrogenase:
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids Included
Missing residues/ Structural gap None / None
Resolution 2.22 Å
Deposition date 2010-12-10
pdb_00003pxt Crystal Structure of Ferrous CO Adduct of MauG in Complex with Pre-Methylamine Dehydrogenase
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids Included
Missing residues/ Structural gap None / None
Resolution 2.16 Å
Deposition date 2010-12-10
pdb_00003pxw Crystal Structure of Ferrous NO Adduct of MauG in Complex with Pre-Methylamine Dehydrogenase
Experimental method X-RAY DIFFRACTION
Structural data available
Non-standard amino acids Included
Missing residues/ Structural gap None / None
Resolution 2.11 Å
Deposition date 2010-12-10