Iron in PDB 2bwh: Laue Structure of A Short Lived State of L29W Myoglobin

The structure of Laue Structure of A Short Lived State of L29W Myoglobin, PDB code: 2bwh was solved by M.Schmidt, K.Nienhaus, R.Pahl, A.Krasselt, S.Anderson, F.Parak, G.U.Nienhaus, V.Srajer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.90
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	91.870, 91.870, 46.040, 90.00, 90.00, 120.00
R / Rfree (%)	23 / 23.3

The binding sites of Iron atom in the Laue Structure of A Short Lived State of L29W Myoglobin (pdb code 2bwh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Laue Structure of A Short Lived State of L29W Myoglobin, PDB code: 2bwh:

Iron binding site 1 out of 1 in the Laue Structure of A Short Lived State of L29W Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Laue Structure of A Short Lived State of L29W Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1154 b:27.3 occ:1.00 FE A:HEM1154 0.0 27.3 1.0 NB A:HEM1154 1.9 15.1 1.0 NA A:HEM1154 2.0 14.8 1.0 NC A:HEM1154 2.0 15.1 1.0 ND A:HEM1154 2.1 15.1 1.0 NE2 A:HIS93 2.2 16.3 1.0 C1B A:HEM1154 3.0 12.9 1.0 C4B A:HEM1154 3.0 14.2 1.0 C4A A:HEM1154 3.0 13.7 1.0 C1C A:HEM1154 3.1 15.5 1.0 C4C A:HEM1154 3.1 17.0 1.0 C1A A:HEM1154 3.1 15.0 1.0 CE1 A:HIS93 3.1 15.6 1.0 C1D A:HEM1154 3.1 14.9 1.0 C4D A:HEM1154 3.2 15.9 1.0 CD2 A:HIS93 3.3 15.7 1.0 CHB A:HEM1154 3.4 13.0 1.0 CHC A:HEM1154 3.4 15.7 1.0 CHD A:HEM1154 3.5 14.0 1.0 CHA A:HEM1154 3.5 13.1 1.0 C3B A:HEM1154 4.2 13.9 1.0 C2B A:HEM1154 4.2 13.9 1.0 C3A A:HEM1154 4.3 16.0 1.0 ND1 A:HIS93 4.3 16.5 1.0 C2A A:HEM1154 4.3 13.1 1.0 C2C A:HEM1154 4.3 17.4 1.0 C3C A:HEM1154 4.4 16.8 1.0 C2D A:HEM1154 4.4 15.8 1.0 CG A:HIS93 4.4 17.2 1.0 C3D A:HEM1154 4.4 16.2 1.0 CE1 A:HIS64 4.5 16.4 1.0 CG2 A:VAL68 4.7 16.3 1.0 NE2 A:HIS64 4.8 20.2 1.0 C A:CMO1155 4.8 42.3 0.6

M.Schmidt, K.Nienhaus, R.Pahl, A.Krasselt, S.Anderson, F.Parak, G.U.Nienhaus, V.Srajer. Ligand Migration Pathway and Protein Dynamics in Myoglobin: A Time-Resolved Crystallographic Study on L29W Mbco. Proc. Natl. Acad. Sci. V. 102 11704 2005U.S.A..
ISSN: ISSN 0027-8424
PubMed: 16085709
DOI: 10.1073/PNAS.0504932102