Iron in PDB 1cci: How Flexible Are Proteins? Trapping of A Flexible Loop

All present enzymatic activity of How Flexible Are Proteins? Trapping of A Flexible Loop:
1.11.1.5;

The structure of How Flexible Are Proteins? Trapping of A Flexible Loop, PDB code: 1cci was solved by Y.Cao, R.A.Musah, S.K.Wilcox, D.B.Goodin, D.E.Mcree, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	107.720, 76.630, 51.680, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the How Flexible Are Proteins? Trapping of A Flexible Loop (pdb code 1cci). 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 How Flexible Are Proteins? Trapping of A Flexible Loop, PDB code: 1cci:

Iron binding site 1 out of 1 in the How Flexible Are Proteins? Trapping of A Flexible Loop


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of How Flexible Are Proteins? Trapping of A Flexible Loop within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:20.8 occ:1.00 FE A:HEM500 0.0 20.8 1.0 O A:HOH313 1.8 18.6 1.0 NE2 A:HIS175 2.0 20.7 1.0 NA A:HEM500 2.1 20.8 1.0 NB A:HEM500 2.1 20.2 1.0 ND A:HEM500 2.1 21.6 1.0 NC A:HEM500 2.1 24.4 1.0 CE1 A:HIS175 2.7 18.5 1.0 C1A A:HEM500 3.0 22.8 1.0 C4A A:HEM500 3.0 21.9 1.0 C1B A:HEM500 3.0 21.5 1.0 C4D A:HEM500 3.1 18.7 1.0 C1D A:HEM500 3.1 18.5 1.0 C4B A:HEM500 3.1 19.8 1.0 C1C A:HEM500 3.1 22.2 1.0 C4C A:HEM500 3.1 22.7 1.0 CD2 A:HIS175 3.1 17.7 1.0 CHA A:HEM500 3.4 21.2 1.0 CHB A:HEM500 3.4 22.3 1.0 CHC A:HEM500 3.4 20.3 1.0 CHD A:HEM500 3.4 16.9 1.0 HE1 A:TRP51 3.4 0.0 1.0 ND1 A:HIS175 3.9 17.8 1.0 NE1 A:TRP51 4.1 21.3 1.0 CG A:HIS175 4.1 16.5 1.0 C2A A:HEM500 4.2 21.6 1.0 C3A A:HEM500 4.2 22.6 1.0 C3D A:HEM500 4.3 15.6 1.0 C2B A:HEM500 4.3 25.1 1.0 C3B A:HEM500 4.3 21.4 1.0 O A:HOH344 4.3 29.9 1.0 C2D A:HEM500 4.3 18.6 1.0 C3C A:HEM500 4.3 18.2 1.0 C2C A:HEM500 4.3 18.9 1.0 O A:HOH300 4.3 27.9 1.0 CD1 A:TRP51 4.5 20.7 1.0 HD1 A:HIS175 4.7 0.0 1.0

M.M.Fitzgerald, R.A.Musah, D.E.Mcree, D.B.Goodin. A Ligand-Gated, Hinged Loop Rearrangement Opens A Channel to A Buried Artificial Protein Cavity. Nat.Struct.Biol. V. 3 626 1996.
ISSN: ISSN 1072-8368
PubMed: 8673607
DOI: 10.1038/NSB0796-626