1b86: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1b86 |SIZE=350|CAPTION= <scene name='initialview01'>1b86</scene>, resolution 2.5Å | |PDB= 1b86 |SIZE=350|CAPTION= <scene name='initialview01'>1b86</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=DDH:[7,12-DEACETYL-3,8,13,17-TETRAMETHYL-21H,23H-PORPHINE-2,18-DIPROPANOATO(2-)-N21,N22,N23,N24]-IRON'>DDH</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=DDH:[7,12-DEACETYL-3,8,13,17-TETRAMETHYL-21H,23H-PORPHINE-2,18-DIPROPANOATO(2-)-N21,N22,N23,N24]-IRON'>DDH</scene>, <scene name='pdbligand=DG2:2,3-DIPHOSPHOGLYCERIC+ACID'>DG2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b86 OCA], [http://www.ebi.ac.uk/pdbsum/1b86 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b86 RCSB]</span> | |||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==Overview== | ||
The haemoglobin-2,3-diphosphoglycerate complex structure has been solved at 2.5 A resolution using crystals grown from low-salt solutions. The results show some important differences with the precedent haemoglobin-2,3-diphosphoglycerate high-salt structure solved by Arnone. First, we observe a loss of symmetry in the binding site, secondly both of the lysine residues 82 beta interact with 2,3-diphosphoglycerate at the same time, each making two contacts. This level of interaction is in agreement with the functional behaviour of natural haemoglobin mutants with mutations at the 2,3-diphosphoglycerate binding site. | The haemoglobin-2,3-diphosphoglycerate complex structure has been solved at 2.5 A resolution using crystals grown from low-salt solutions. The results show some important differences with the precedent haemoglobin-2,3-diphosphoglycerate high-salt structure solved by Arnone. First, we observe a loss of symmetry in the binding site, secondly both of the lysine residues 82 beta interact with 2,3-diphosphoglycerate at the same time, each making two contacts. This level of interaction is in agreement with the functional behaviour of natural haemoglobin mutants with mutations at the 2,3-diphosphoglycerate binding site. | ||
==About this Structure== | ==About this Structure== | ||
| Line 28: | Line 28: | ||
[[Category: Mauguen, Y.]] | [[Category: Mauguen, Y.]] | ||
[[Category: Richard, V.]] | [[Category: Richard, V.]] | ||
[[Category: 2]] | [[Category: 2]] | ||
[[Category: 3-diphosphoglycerate]] | [[Category: 3-diphosphoglycerate]] | ||
| Line 36: | Line 33: | ||
[[Category: haemoglobin]] | [[Category: haemoglobin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:55:34 2008'' | ||