2HBG

GLYCERA DIBRANCHIATA HEMOGLOBIN. STRUCTURE AND REFINEMENT AT 1.5 ANGSTROMS RESOLUTION

Summary for 2HBG

• Entry DOI: 10.2210/pdb2hbg/pdb
• Descriptor: HEMOGLOBIN (DEOXY), PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: oxygen transport
• Biological source: Glycera dibranchiata
• Total number of polymer chains: 1
• Total formula weight: 15551.72

Authors

Arents, G.A.,Love, W.E. (deposition date: 1991-02-11, release date: 1992-07-15, Last modification date: 2024-02-14)

Primary citation

Arents, G.,Love, W.E.
Glycera dibranchiata hemoglobin. Structure and refinement at 1.5 A resolution.
J.Mol.Biol., 210:149-161, 1989

PubMed Abstract: The coelomic cells of the common marine bloodworm Glycera dibranchiata contain several hemoglobin monomers and polydisperse polymers. We present the refined structure of one of the Glycera monomers at 1.5 A resolution. The molecular model for protein and ordered solvent for the deoxy form of the Glycera monomer has been refined to a crystallographic R-factor of 12.7% against an X-ray diffraction dataset at 1.5 A resolution. The positions of 1095 protein atoms have been determined with a maximum root-mean-square (r.m.s.) error of 0.13 A, and the r.m.s. deviation from ideal bond lengths is 0.015 A and from ideal bond angles is 1.0 degree. The r.m.s. deviation of planar groups from their least-squares planes is 0.007 A, and the r.m.s. deviation for torsion angles is 1.2 degrees for peptide groups and 16.8 degrees for side-chains. A total of 153 water molecules has been located, and they have been refined to a final average occupancy of 0.80. Multiple conformations have been found for five side-chains, and a change has been suggested for the sequence at five residues. The heme group is present in the "reverse" orientation that differs only in the positions of the vinyl beta-carbons from the "normal" orientation. The doming of the heme towards the proximal side, and the bond distances and angles of the heme and proximal histidine are typical of most deoxy globin structures. The substitution of leucine for the distal histidine residue (E7) creates an unusually hydrophobic heme pocket.

PubMed: 2585515
DOI: 10.1016/0022-2836(89)90297-0

Experimental method

X-RAY DIFFRACTION (1.5 Å)