Iron in PDB 2nwb: Crystal Structure of A Putative 2,3-Dioxygenase (SO4414) From Shewanella Oneidensis in Complex with Ferric Heme. Northeast Structural Genomics Target SOR52.

The structure of Crystal Structure of A Putative 2,3-Dioxygenase (SO4414) From Shewanella Oneidensis in Complex with Ferric Heme. Northeast Structural Genomics Target SOR52., PDB code: 2nwb was solved by F.Forouhar, J.L.R.Anderson, C.G.Mowat, A.Hussain, J.Seetharaman, C.Bruckmann, S.J.Thackray, N.Khan, K.Cunningham, H.Janjua, L.Zhao, R.Xiao, L.C.Ma, J.Liu, M.C.Baran, T.B.Acton, B.Rost, G.T.Montelione, S.K.Champman, L.Tong, Northeast Structural Genomics Consortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.99 / 2.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	138.851, 68.698, 87.790, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 22.5

The binding sites of Iron atom in the Crystal Structure of A Putative 2,3-Dioxygenase (SO4414) From Shewanella Oneidensis in Complex with Ferric Heme. Northeast Structural Genomics Target SOR52. (pdb code 2nwb). 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 Crystal Structure of A Putative 2,3-Dioxygenase (SO4414) From Shewanella Oneidensis in Complex with Ferric Heme. Northeast Structural Genomics Target SOR52., PDB code: 2nwb:

Iron binding site 1 out of 1 in the Crystal Structure of A Putative 2,3-Dioxygenase (SO4414) From Shewanella Oneidensis in Complex with Ferric Heme. Northeast Structural Genomics Target SOR52.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of A Putative 2,3-Dioxygenase (SO4414) From Shewanella Oneidensis in Complex with Ferric Heme. Northeast Structural Genomics Target SOR52. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:34.8 occ:1.00 FE A:HEM401 0.0 34.8 1.0 ND A:HEM401 2.0 36.7 1.0 NA A:HEM401 2.1 36.7 1.0 NB A:HEM401 2.1 36.7 1.0 NC A:HEM401 2.1 36.7 1.0 NE2 A:HIS324 2.5 26.6 1.0 C1D A:HEM401 3.0 39.6 1.0 C4D A:HEM401 3.0 42.8 1.0 C1B A:HEM401 3.0 39.3 1.0 C1A A:HEM401 3.0 41.9 1.0 C4A A:HEM401 3.0 40.1 1.0 C4C A:HEM401 3.1 47.0 1.0 CD2 A:HIS324 3.1 28.0 1.0 C4B A:HEM401 3.2 42.4 1.0 C1C A:HEM401 3.2 50.2 1.0 CHA A:HEM401 3.4 46.5 1.0 CHB A:HEM401 3.4 46.3 1.0 CHD A:HEM401 3.4 43.9 1.0 CHC A:HEM401 3.5 36.6 1.0 O A:HOH402 3.5 11.7 1.0 CE1 A:HIS324 3.6 28.6 1.0 C2D A:HEM401 4.2 38.9 1.0 C3D A:HEM401 4.2 40.1 1.0 C3A A:HEM401 4.3 43.5 1.0 C2A A:HEM401 4.3 43.2 1.0 C2B A:HEM401 4.3 45.1 1.0 CB A:ALA236 4.4 32.1 1.0 C3B A:HEM401 4.4 49.0 1.0 C3C A:HEM401 4.4 48.8 1.0 C2C A:HEM401 4.4 50.6 1.0 CG A:HIS324 4.4 30.4 1.0 ND1 A:HIS324 4.6 30.8 1.0 N A:ALA236 4.9 32.7 1.0

F.Forouhar, J.L.Anderson, C.G.Mowat, S.M.Vorobiev, A.Hussain, M.Abashidze, C.Bruckmann, S.J.Thackray, J.Seetharaman, T.Tucker, R.Xiao, L.C.Ma, L.Zhao, T.B.Acton, G.T.Montelione, S.K.Chapman, L.Tong. Molecular Insights Into Substrate Recognition and Catalysis By Tryptophan 2,3-Dioxygenase. Proc.Natl.Acad.Sci.Usa V. 104 473 2007.
ISSN: ISSN 0027-8424
PubMed: 17197414
DOI: 10.1073/PNAS.0610007104