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Iron in PDB 2r6s: Crystal Structure of Gab Protein

Protein crystallography data

The structure of Crystal Structure of Gab Protein, PDB code: 2r6s was solved by B.Lohkamp, D.Dobritzsch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.36 / 2.10
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 120.900, 120.900, 137.170, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 19.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Gab Protein (pdb code 2r6s). 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 Gab Protein, PDB code: 2r6s:

Iron binding site 1 out of 1 in 2r6s

Go back to Iron Binding Sites List in 2r6s
Iron binding site 1 out of 1 in the Crystal Structure of Gab Protein


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 Gab Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:27.0
occ:1.00
O6 A:BCN505 2.1 34.5 1.0
O22 A:BCN505 2.1 37.0 1.0
NE2 A:HIS292 2.1 29.1 1.0
NE2 A:HIS160 2.1 27.6 1.0
N1 A:BCN505 2.2 35.3 1.0
OD1 A:ASP162 2.2 29.9 1.0
C2 A:BCN505 2.8 39.7 1.0
C1 A:BCN505 2.9 37.6 1.0
C6 A:BCN505 3.0 34.2 1.0
C5 A:BCN505 3.0 33.5 1.0
C3 A:BCN505 3.0 35.3 1.0
CE1 A:HIS292 3.0 32.1 1.0
CD2 A:HIS292 3.1 32.5 1.0
CG A:ASP162 3.1 32.1 1.0
CD2 A:HIS160 3.1 28.4 1.0
CE1 A:HIS160 3.1 28.8 1.0
OD2 A:ASP162 3.3 32.5 1.0
O21 A:BCN505 4.0 41.1 1.0
ND1 A:HIS292 4.1 28.6 1.0
O A:HOH602 4.1 17.5 0.5
CG A:HIS292 4.2 30.0 1.0
ND1 A:HIS160 4.2 26.1 1.0
CG A:HIS160 4.2 28.6 1.0
C4 A:BCN505 4.4 35.2 1.0
CB A:ASP162 4.5 31.9 1.0
CE A:MET175 4.7 32.1 0.3
N A:ASP162 4.9 31.2 1.0
CA A:ASP162 4.9 31.6 1.0
O1 A:SO4502 4.9 55.2 1.0

Reference:

B.Lohkamp, D.Dobritzsch. A Mixture of Fortunes: the Curious Determination of the Structure of Escherichia Coli BL21 Gab Protein. Acta Crystallogr.,Sect.D V. 64 407 2008.
ISSN: ISSN 0907-4449
PubMed: 18391407
DOI: 10.1107/S0907444908001091
Page generated: Thu Jul 17 03:54:24 2025

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