PDBsum entry 1ymc

Oxygen transport

PDB id

1ymc

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Contents

			Protein chain

					153 a.a. *

			Ligands

					SO4


					CYN-CLN

			Waters ×173

* Residue conservation analysis

PDB id:

1ymc

Links

Name:

Oxygen transport

Title:

Three-dimensional structure of cyanomet-sulfmyoglobin c

Structure:

Cyanomet-sulfmyoglobin. Chain: a. Engineered: yes

Source:

Equus caballus. Horse. Organism_taxid: 9796

Resolution:

2.00Å

R-factor:

0.129

Authors:

S.V.Evans,G.D.Brayer

Key ref:

S.V.Evans et al. (1994). Three-dimensional structure of cyanomet-sulfmyoglobin C. Proc Natl Acad Sci U S A, 91, 4723-4726. PubMed id: 8197124 DOI: 10.1073/pnas.91.11.4723

Date:

27-Sep-93

Release date:

31-Jan-94

PROCHECK

	Headers

	References

Protein chain

P68082 (MYG_HORSE) - Myoglobin from Equus caballus

Seq: Struc:					154 a.a. 153 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1073/pnas.91.11.4723	Proc Natl Acad Sci U S A 91:4723-4726 (1994)
PubMed id: 8197124

Three-dimensional structure of cyanomet-sulfmyoglobin C.
S.V.Evans, B.P.Sishta, A.G.Mauk, G.D.Brayer.

ABSTRACT

The atomic structure of horse heart cyanomet-sulfmyoglobin C has been established by x-ray crystallographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfmyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sulfur atom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21298302

F.P.Nicoletti, M.K.Thompson, S.Franzen, and G.Smulevich (2011).
Degradation of sulfide by dehaloperoxidase-hemoglobin from Amphitrite ornata.

J Biol Inorg Chem, 16, 611-619.

17554165

M.Sugishima, K.Oda, T.Ogura, H.Sakamoto, M.Noguchi, and K.Fukuyama (2007).
Alternative cyanide-binding modes to the haem iron in haem oxygenase.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 471-474.

PDB code:

2e7e

10423453

M.Bolognesi, C.Rosano, R.Losso, A.Borassi, M.Rizzi, J.B.Wittenberg, A.Boffi, and P.Ascenzi (1999).
Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study.

Biophys J, 77, 1093-1099.

PDB codes:

1b0b 1ebc 1ebt

9032082

K.S.Kroeger, and C.E.Kundrot (1997).
Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins.

Structure, 5, 227-237.

PDB codes:

1abw 1aby

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.