1mbn Summary


The stereochemistry of the protein myoglobin

The structure was published by Watson, H.C., in 1969 in a paper entitled "The Stereochemistry of the Protein Myoglobin" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1973.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of MYOGLOBIN. This molecule has the UniProt identifier P02185 (MYG_PHYCD)search. The sample contained 153 residues which is 99% of the natural sequence. Out of 153 residues 152 were observed and are deposited in the PDB.

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 is most likely monomeric.

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 P02185 (2-154) (MYG_PHYCD)search Physeter catodonsearch 98% 153 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P02185 (2 - 154) MYOGLOBIN Physeter catodon

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P02185) Globinssearch Globinssearch PF00042: Globinsearch

Chain ID Biological process (GO) Molecular function (GO)
A (P02185) oxygen transportsearch transportsearch oxygen bindingsearch iron ion bindingsearch metal ion bindingsearch heme bindingsearch oxygen transporter activitysearch

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