Iron in PDB 1ywd: 1.08 A Structure of Ferrous NP4 (Aquo Complex)

The structure of 1.08 A Structure of Ferrous NP4 (Aquo Complex), PDB code: 1ywd was solved by E.M.Maes, A.Weichsel, S.A.Roberts, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.08
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	70.063, 42.905, 52.272, 90.00, 94.37, 90.00
R / Rfree (%)	14.1 / 17

The binding sites of Iron atom in the 1.08 A Structure of Ferrous NP4 (Aquo Complex) (pdb code 1ywd). 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 1.08 A Structure of Ferrous NP4 (Aquo Complex), PDB code: 1ywd:

Iron binding site 1 out of 1 in the 1.08 A Structure of Ferrous NP4 (Aquo Complex)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.08 A Structure of Ferrous NP4 (Aquo Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe185 b:9.2 occ:1.00 FE A:HEM185 0.0 9.2 1.0 NB A:HEM185 2.0 9.6 1.0 ND A:HEM185 2.0 10.4 1.0 NC A:HEM185 2.0 10.1 1.0 NE2 A:HIS59 2.0 9.0 1.0 NA A:HEM185 2.0 8.7 1.0 O A:HOH186 2.2 20.1 1.0 CE1 A:HIS59 3.0 8.5 1.0 C4B A:HEM185 3.0 10.3 1.0 C1C A:HEM185 3.0 11.0 1.0 C4A A:HEM185 3.0 8.5 1.0 C1A A:HEM185 3.0 8.9 1.0 C4C A:HEM185 3.1 11.1 1.0 C1B A:HEM185 3.1 9.2 1.0 CD2 A:HIS59 3.1 9.4 1.0 C1D A:HEM185 3.1 11.8 1.0 C4D A:HEM185 3.1 10.5 1.0 CHC A:HEM185 3.4 11.0 1.0 CHA A:HEM185 3.4 9.9 1.0 CHB A:HEM185 3.4 9.1 1.0 CHD A:HEM185 3.5 11.5 1.0 ND1 A:HIS59 4.1 8.4 1.0 CG A:HIS59 4.2 8.6 1.0 C3B A:HEM185 4.2 10.1 1.0 C3A A:HEM185 4.3 8.7 1.0 C2A A:HEM185 4.3 9.0 1.0 C3D A:HEM185 4.3 12.6 1.0 C2D A:HEM185 4.3 13.5 1.0 C3C A:HEM185 4.3 13.4 1.0 C2C A:HEM185 4.3 13.0 1.0 O A:HOH433 4.3 33.7 1.0 C2B A:HEM185 4.3 10.2 1.0 O A:HOH383 5.0 20.0 1.0

E.M.Maes, S.A.Roberts, A.Weichsel, W.R.Montfort. Ultrahigh Resolution Structures of Nitrophorin 4: Heme Distortion in Ferrous Co and No Complexes Biochemistry V. 44 12690 2005.
ISSN: ISSN 0006-2960
PubMed: 16171383
DOI: 10.1021/BI0506573