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Iron in PDB 1v07: Crystal Structure of THRE11VAL Mutant of the Nerve Tissue Mini-Hemoglobin From the Nemertean Worm Cerebratulus Lacteus

Protein crystallography data

The structure of Crystal Structure of THRE11VAL Mutant of the Nerve Tissue Mini-Hemoglobin From the Nemertean Worm Cerebratulus Lacteus, PDB code: 1v07 was solved by A.Pesce, M.Nardini, P.Ascenzi, E.Geuens, S.Dewilde, L.Moens, M.Bolognesi, A.Riggs, A.Hale, P.Deng, G.U.Nienhaus, J.S.Olson, K.Nienhaus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.0 / 1.7
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.656, 43.422, 59.660, 90.00, 90.00, 90.00
R / Rfree (%) 16.737 / 19.526

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of THRE11VAL Mutant of the Nerve Tissue Mini-Hemoglobin From the Nemertean Worm Cerebratulus Lacteus (pdb code 1v07). 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 THRE11VAL Mutant of the Nerve Tissue Mini-Hemoglobin From the Nemertean Worm Cerebratulus Lacteus, PDB code: 1v07:

Iron binding site 1 out of 1 in 1v07

Go back to Iron Binding Sites List in 1v07
Iron binding site 1 out of 1 in the Crystal Structure of THRE11VAL Mutant of the Nerve Tissue Mini-Hemoglobin From the Nemertean Worm Cerebratulus Lacteus


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 THRE11VAL Mutant of the Nerve Tissue Mini-Hemoglobin From the Nemertean Worm Cerebratulus Lacteus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe144

b:15.7
occ:1.00
FE A:HEM144 0.0 15.7 1.0
O2 A:OXY150 1.9 20.6 1.0
ND A:HEM144 2.0 13.3 1.0
NA A:HEM144 2.0 15.4 1.0
NB A:HEM144 2.0 14.8 1.0
NC A:HEM144 2.1 15.3 1.0
NE2 A:HIS69 2.1 13.0 1.0
O1 A:OXY150 2.5 36.1 1.0
CE1 A:HIS69 3.0 15.8 1.0
C4D A:HEM144 3.0 14.7 1.0
C1A A:HEM144 3.0 13.2 1.0
C1D A:HEM144 3.0 14.5 1.0
C4A A:HEM144 3.0 14.1 1.0
C4B A:HEM144 3.1 17.1 1.0
C1B A:HEM144 3.1 13.0 1.0
C4C A:HEM144 3.1 15.4 1.0
C1C A:HEM144 3.1 17.3 1.0
CD2 A:HIS69 3.1 12.7 1.0
CHA A:HEM144 3.4 15.4 1.0
CHB A:HEM144 3.4 14.4 1.0
CHD A:HEM144 3.4 15.8 1.0
CHC A:HEM144 3.4 16.9 1.0
ND1 A:HIS69 4.2 14.9 1.0
CG A:HIS69 4.2 15.1 1.0
C3A A:HEM144 4.3 13.7 1.0
NE2 A:GLN44 4.3 18.4 1.0
C3D A:HEM144 4.3 16.8 1.0
C2A A:HEM144 4.3 13.4 1.0
C3B A:HEM144 4.3 16.3 1.0
C2D A:HEM144 4.3 14.6 1.0
C2B A:HEM144 4.3 15.5 1.0
C3C A:HEM144 4.3 17.1 1.0
C2C A:HEM144 4.3 17.7 1.0
CZ A:PHE25 4.7 16.8 1.0
OH A:TYR11 4.7 24.5 1.0
CE2 A:PHE25 4.8 15.9 1.0
CZ A:PHE79 4.9 16.4 1.0

Reference:

A.Pesce, M.Nardini, P.Ascenzi, E.Geuens, S.Dewilde, L.Moens, M.Bolognesi, A.Riggs, A.Hale, P.Deng, G.U.Nienhaus, J.S.Olson, K.Nienhaus. Thr-E11 Regulates O2 Affinity in Cerebratulus Lacteus Mini-Hemoglobin J.Biol.Chem. V. 279 33662 2004.
ISSN: ISSN 0021-9258
PubMed: 15161908
DOI: 10.1074/JBC.M403597200
Page generated: Sat Aug 3 16:07:00 2024

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