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PDBsum entry 1ecd

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Oxygen transport PDB id
1ecd
Contents
Protein chain
136 a.a.
Ligands
HEM
Waters ×95

References listed in PDB file
Key reference
Title Structure of erythrocruorin in different ligand states refined at 1.4 a resolution.
Authors W.Steigemann, E.Weber.
Ref. J Mol Biol, 1979, 127, 309-338. [DOI no: 10.1016/0022-2836(79)90332-2]
PubMed id 430568
Abstract
No abstract given.
Figure 7.
FIG. 7. Stereoscopic drawin of the haem group and its environment in met-erythrocruorin. The iron-ligand bonds are shown by thin lins. The bond to the water molecule is dashed, since it. is 3 A from th iron and may not really be co-ordinated to it. Polar linkages of the haem to t,hc globin and hydrogen bonds involving water molecules are represented by thin lines.
Figure 8.
FIG. 8. Difference Fourier maps with coefficients iF,(deri)/ - lF,(deoxy)l, c,(deoxy), where PJderi) are the observed structure factors of the ligation form aquomet, cerbonmonoxy, and cyaomet, respectively. The oc,(deoxy) are the calcuated phases of the refined deoxy model. Composite drawing of several sections projected parallel to the haem plane, represented by the heevy line. The vinyl-substit)uted pyrrole residues are pointing awa from the observer. The distal ide is on the left, the proximal on the right. Positive density is dran with solid lies, negative with broken lines. Contour lines beginning at 0.16 eAms with a separation of 0.08 eA-3. (a) Coefficients lE'',(aquomet) 1 - lF,(deoxy) 1, a,(deoxy). (b) Coefficients lP,(crtrbonmonoxy) 1 - IP,(deoxy) 1, cc,(deoxy). (0) Coefficients IF, (oyanomet) 1 - lF,(deoxy) /, cr,(deoxy).
The above figures are reprinted by permission from Elsevier: J Mol Biol (1979, 127, 309-338) copyright 1979.
Secondary reference #1
Title The structure of oxy-Erythrocruorin at 1.4 x resolution.
Authors E.Weber, W.Steigemann, T.A.Jones, R.Huber.
Ref. J Mol Biol, 1978, 120, 327-336. [DOI no: 10.1016/0022-2836(78)90071-2]
PubMed id 642012
Full text Abstract
Figure 3.
PIG. 3. Difference Fourier map with coefficients ([FO,oxYI-l 1'',,,,,,,-,,,1), ~~,nso~r-~~~~, where I~``.OXYI are the observed structure factor amplitudes of the oxygenated form, 1 F,,,so,, _ uaol arc tho calclated structure factor amplitudes of the deoxy model oming the half occupied deoxy- water molecule, and ~~,nso~r-s~o are calculated phases of this model. Comosite drawing of several sections projected parallel to the haem plane. The vinyl-substituted pyrrol residues are pointing way from the observer (see Fig. 6). Positive density drawn with solid lines, negative with roken line. Contour lines beginning at 0.16 e Am3 with a separation of 0.08 e Ae3. A model nterpretation is overlaid.
Figure 6.
FIG. 6. Stereoscopic view of haem and lignds in the oxy model. The view is as those in the Fourier maps.
The above figures are reproduced from the cited reference with permission from Elsevier
Secondary reference #2
Title The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin.
Authors R.Huber, O.Epp, W.Steigemann, H.Formanek.
Ref. Eur J Biochem, 1971, 19, 42-50.
PubMed id 5102553
Abstract
Secondary reference #3
Title Structures of deoxy- And carbonmonoxy-Erythrocruorin.
Authors R.Huber, O.Epp, H.Formanek.
Ref. J Mol Biol, 1970, 52, 349-354.
PubMed id 5485913
Abstract
PROCHECK
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