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PDBsum entry 451c

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Electron transport PDB id
451c
Contents
Protein chain
82 a.a.
Ligands
HEM
Waters ×73

References listed in PDB file
Key reference
Title Structure of cytochrome c551 from pseudomonas aeruginosa refined at 1.6 a resolution and comparison of the two redox forms.
Authors Y.Matsuura, T.Takano, R.E.Dickerson.
Ref. J Mol Biol, 1982, 156, 389-409. [DOI no: 10.1016/0022-2836(82)90335-7]
PubMed id 6283101
Abstract
No abstract given.
Figure 3.
FIG. 3. All theside-chains onan a-carbon skeleton. (a) Front view, and (b) view from Met61 aide. Not.e a long sequence of hydrophobic residues along the edge of heme crevice on the Met61 side.
Figure 9.
FIG. 9. Hydrogen-bod network among water molecules (WAT) 11. 23 and 25. LyslOCO Ile48CO. ro62C0, sn64Nd and 06 MetGlS, and Ala65NH in the heme crevice of the reduced frm. Probable ydrogens are indicated by thick lines on hydrogen bonds. Circles adjacent to water molecules 23 ad 25 indicate their positions in the oxidized form.
The above figures are reprinted by permission from Elsevier: J Mol Biol (1982, 156, 389-409) copyright 1982.
Secondary reference #1
Title Pseudomonas cytochrome c551 at 2.0 a resolution: enlargement of the cytochrome c family.
Authors R.J.Almassy, R.E.Dickerson.
Ref. Proc Natl Acad Sci U S A, 1978, 75, 2674-2678. [DOI no: 10.1073/pnas.75.6.2674]
PubMed id 96440
Full text Abstract
Secondary reference #2
Title The cytochrome fold and the evolution of bacterial energy metabolism.
Authors R.E.Dickerson, R.Timkovich, R.J.Almassy.
Ref. J Mol Biol, 1976, 100, 473-491.
PubMed id 176369
Abstract
PROCHECK
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