1B86

HUMAN DEOXYHAEMOGLOBIN-2,3-DIPHOSPHOGLYCERATE COMPLEX

Summary for 1B86

• Entry DOI: 10.2210/pdb1b86/pdb
• Descriptor: PROTEIN (HEMOGLOBIN; ALPHA CHAIN), PROTEIN (HEMOGLOBIN; BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: allosteric effector, 2, 3-diphosphoglycerate, oxygen transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 64877.08

Authors

Richard, V.,Dodson, G.G.,Mauguen, Y. (deposition date: 1999-02-08, release date: 1999-02-14, Last modification date: 2024-05-22)

Primary citation

Richard, V.,Dodson, G.G.,Mauguen, Y.
Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution.
J.Mol.Biol., 233:270-274, 1993

PubMed Abstract: 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.

PubMed: 8377203
DOI: 10.1006/jmbi.1993.1505

Experimental method

X-RAY DIFFRACTION (2.5 Å)