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| | <StructureSection load='3g46' size='340' side='right'caption='[[3g46]], [[Resolution|resolution]] 0.91Å' scene=''> | | <StructureSection load='3g46' size='340' side='right'caption='[[3g46]], [[Resolution|resolution]] 0.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g46]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anain Anain]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G46 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G46 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g46]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anadara_inaequivalvis Anadara inaequivalvis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G46 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.91Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sdh|3sdh]], [[4sdh|4sdh]], [[3g4q|3g4q]], [[3g4r|3g4r]], [[3g4u|3g4u]], [[3g4v|3g4v]], [[3g4w|3g4w]], [[3g4y|3g4y]], [[3g52|3g52]], [[3g53|3g53]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HBI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6561 ANAIN])</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=3g46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g46 OCA], [https://pdbe.org/3g46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g46 RCSB], [https://www.ebi.ac.uk/pdbsum/3g46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g46 ProSAT]</span></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=3g46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g46 OCA], [http://pdbe.org/3g46 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g46 RCSB], [http://www.ebi.ac.uk/pdbsum/3g46 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g46 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GLB1_ANAIN GLB1_ANAIN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anain]] | + | [[Category: Anadara inaequivalvis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cohen, J]] | + | [[Category: Cohen J]] |
| - | [[Category: Gibson, Q H]] | + | [[Category: Gibson QH]] |
| - | [[Category: Knapp, J E]] | + | [[Category: Knapp JE]] |
| - | [[Category: Nichols, J C]] | + | [[Category: Nichols JC]] |
| - | [[Category: Pahl, R]] | + | [[Category: Pahl R]] |
| - | [[Category: Royer, W E]] | + | [[Category: Royer Jr WE]] |
| - | [[Category: Schulten, K]] | + | [[Category: Schulten K]] |
| - | [[Category: Srajer, V]] | + | [[Category: Srajer V]] |
| - | [[Category: Allostery]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Oxygen affinity]]
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| - | [[Category: Oxygen binding]]
| + | |
| - | [[Category: Oxygen storage/transport]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Transport]]
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| Structural highlights
Function
GLB1_ANAIN
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
As in many other hemoglobins, no direct route for migration of ligands between solvent and active site is evident from crystal structures of Scapharca inaequivalvis dimeric HbI. Xenon (Xe) and organic halide binding experiments, along with computational analysis presented here, reveal protein cavities as potential ligand migration routes. Time-resolved crystallographic experiments show that photodissociated carbon monoxide (CO) docks within 5 ns at the distal pocket B site and at more remote Xe4 and Xe2 cavities. CO rebinding is not affected by the presence of dichloroethane within the major Xe4 protein cavity, demonstrating that this cavity is not on the major exit pathway. The crystal lattice has a substantial influence on ligand migration, suggesting that significant conformational rearrangements may be required for ligand exit. Taken together, these results are consistent with a distal histidine gate as one important ligand entry and exit route, despite its participation in the dimeric interface.
Ligand migration and cavities within Scapharca Dimeric HbI: studies by time-resolved crystallo-graphy, Xe binding, and computational analysis.,Knapp JE, Pahl R, Cohen J, Nichols JC, Schulten K, Gibson QH, Srajer V, Royer WE Jr Structure. 2009 Nov 11;17(11):1494-504. PMID:19913484[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Knapp JE, Pahl R, Cohen J, Nichols JC, Schulten K, Gibson QH, Srajer V, Royer WE Jr. Ligand migration and cavities within Scapharca Dimeric HbI: studies by time-resolved crystallo-graphy, Xe binding, and computational analysis. Structure. 2009 Nov 11;17(11):1494-504. PMID:19913484 doi:10.1016/j.str.2009.09.004
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