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2hmz

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THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION

Structural highlights

2hmz is a 4 chain structure with sequence from Dendrostomum dyscritum. This structure supersedes the now removed PDB entry 1hmz. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HEMT_THEDY] Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact.

Structures of met and azidomet hemerythrin at 1.66 A resolution.,Holmes MA, Stenkamp RE J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:1870128^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Holmes MA, Stenkamp RE. Structures of met and azidomet hemerythrin at 1.66 A resolution. J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:1870128

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hmz"

Categories: Dendrostomum dyscritum | Large Structures | Holmes, M A | Stenkamp, R E | Oxygen transport

@@ Line 3: / Line 3: @@
 <StructureSection load='2hmz' size='340' side='right'caption='[[2hmz]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2hmz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dendrostomum_dyscritum Dendrostomum dyscritum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hmz 1hmz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HMZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2hmz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendrostomum_dyscritum Dendrostomum dyscritum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hmz 1hmz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HMZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FEA:MONOAZIDO-MU-OXO-DIIRON'>FEA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FEA:MONOAZIDO-MU-OXO-DIIRON'>FEA</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmz OCA], [http://pdbe.org/2hmz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hmz RCSB], [http://www.ebi.ac.uk/pdbsum/2hmz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hmz ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmz OCA], [https://pdbe.org/2hmz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hmz RCSB], [https://www.ebi.ac.uk/pdbsum/2hmz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hmz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEMT_THEDY HEMT_THEDY]] Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.
+[[https://www.uniprot.org/uniprot/HEMT_THEDY HEMT_THEDY]] Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2hmz

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THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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