3vm9 Summary


Dimeric horse myoglobin

The structure was published by Nagao, S., Osuka, H., Yamada, T., et al., Imai, K., Higuchi, Y., and Hirota, S., in 2012 in a paper entitled "Structural and oxygen binding properties of dimeric horse myoglobin" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.05 Å and deposited in 2011.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Myoglobin.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Myoglobin P68082 (2-154) (MYG_HORSE)search Equus caballussearch 99% 153 100%
B Myoglobin P68082 (2-154) (MYG_HORSE)search Equus caballussearch 99% 153 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P68082 (2 - 154) Myoglobin Equus caballus

Chain Sequence family (Pfam)
A, B (P68082) PF00042: Globinsearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P68082) transportsearch enucleate erythrocyte differentiationsearch oxygen transportsearch brown fat cell differentiationsearch heart developmentsearch response to hypoxiasearch heme bindingsearch iron ion bindingsearch oxygen bindingsearch oxygen transporter activitysearch metal ion bindingsearch

Chain InterPro annotation
A, B Globinsearch Myoglobinsearch Globin-likesearch Globin, structural domainsearch