1S0H

Structure determination of haemoglobin from Donkey(equus asinus) at 3.0 Angstrom resolution

Summary for 1S0H

• Entry DOI: 10.2210/pdb1s0h/pdb
• Descriptor: Hemoglobin alpha chain, Hemoglobin beta chain, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: alpha helix, dimer, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Equus asinus (ass); More
• Total number of polymer chains: 2
• Total formula weight: 32363.48

Authors

Balasundaresan, D.,Ponnuswamy, M.N.,Saraboji, K. (deposition date: 2003-12-31, release date: 2005-02-01, Last modification date: 2023-10-25)

Primary citation

Balasundaresan, D.,Saraboji, K.,Ponnuswamy, M.N.
Crystal structure of haemoglobin from donkey (Equus asinus) at 3A resolution
Biochimie, 88:719-723, 2006

PubMed Abstract: Haemoglobin from donkey was purified and crystallized in space group C2. The present donkey haemoglobin model comprises of two subunits alpha and beta. These alpha and beta subunits comprise of 141 and 146 amino acid residues, respectively, and the haem groups. The donkey haemoglobin differs from horse only in two amino acids of alpha-chain (His20 to Asn and Tyr24 to Phe) and these substitutions do not significantly change the secondary structural features of donkey haemoglobin. The haem group region and subunit contacts are closely resemble with that of horse methaemoglobin.

PubMed: 16488065
DOI: 10.1016/j.biochi.2006.01.001

Experimental method

X-RAY DIFFRACTION (3 Å)