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TitleLigand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: roles of TyrB10 and GlnE11 residues
Journal, issue, pagesBiochemistry, Vol. 45, Page 8770-8781, Year 2006
Publish dateApr 3, 2006 (structure data deposition date)
AuthorsOuellet, Y. / Milani, M. / Couture, M. / Bolognesi, M. / Guertin, M.
External linksBiochemistry / PubMed:16846220
MethodsX-ray diffraction
Resolution1.731 - 2.1 Å
Structure data

PDB-2gkm:
Crystal structure of Mycobacterium tuberculosis trHbN TyrB10Phe mutant
Method: X-RAY DIFFRACTION / Resolution: 1.731 Å

PDB-2gkn:
Crystal structure of Mycobacterium tuberculosis trHbN, GlnE11Val mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2gl3:
Crystal structure of Mycobacterium tuberculosis trHbN, TyrB10Phe GlnE11Val mutant
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

PDB-2gln:
Crystal structure of Mycobacterium tuberculosis trHbN, GlnE11Ala mutant
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-CYN:
CYANIDE ION

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsOXYGEN STORAGE/TRANSPORT / truncated hemoglobin; mutant / OXYGEN STORAGE-TRANSPORT COMPLEX

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