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Iron in PDB 4m51: Crystal Structure of Amidohydrolase NIS_0429 (SER145ALA Mutant) From Nitratiruptor Sp. SB155-2

Protein crystallography data

The structure of Crystal Structure of Amidohydrolase NIS_0429 (SER145ALA Mutant) From Nitratiruptor Sp. SB155-2, PDB code: 4m51 was solved by Y.Patskovsky, R.Toro, A.Gobble, F.M.Raushel, S.C.Almo, Enzyme Functioninitiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.91 / 1.08
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 92.163, 75.788, 76.291, 90.00, 120.99, 90.00
R / Rfree (%) 11.7 / 13.5

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Amidohydrolase NIS_0429 (SER145ALA Mutant) From Nitratiruptor Sp. SB155-2 (pdb code 4m51). 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 Amidohydrolase NIS_0429 (SER145ALA Mutant) From Nitratiruptor Sp. SB155-2, PDB code: 4m51:

Iron binding site 1 out of 1 in 4m51

Go back to Iron Binding Sites List in 4m51
Iron binding site 1 out of 1 in the Crystal Structure of Amidohydrolase NIS_0429 (SER145ALA Mutant) From Nitratiruptor Sp. SB155-2


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 Amidohydrolase NIS_0429 (SER145ALA Mutant) From Nitratiruptor Sp. SB155-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe503

b:14.2
occ:0.51
O A:HOH962 1.6 14.7 1.0
NE2 A:HIS61 2.0 13.1 1.0
NE2 A:HIS63 2.1 19.4 1.0
NE2 A:HIS206 2.3 13.7 1.0
OD1 A:ASP306 2.5 13.3 0.5
CD2 A:HIS63 2.8 16.3 1.0
CE1 A:HIS61 2.9 11.9 1.0
CD2 A:HIS61 3.0 12.3 1.0
CD2 A:HIS206 3.0 12.9 1.0
CE1 A:HIS63 3.3 17.8 1.0
O A:HOH1037 3.3 22.6 0.5
OD1 A:ASP306 3.3 12.8 0.5
O A:HOH1037 3.5 17.3 0.5
CE1 A:HIS206 3.5 13.7 1.0
CG A:ASP306 3.6 12.9 0.5
CG A:ASP306 3.8 12.6 0.5
OD2 A:ASP306 3.8 14.3 0.5
OD2 A:ASP306 3.9 12.6 0.5
NE2 A:HIS257 4.0 10.9 1.0
ND1 A:HIS61 4.0 11.8 1.0
O A:HOH932 4.0 20.5 1.0
CG A:HIS63 4.1 13.8 1.0
CG A:HIS61 4.1 11.4 1.0
ND1 A:HIS63 4.2 15.3 1.0
CG A:HIS206 4.3 10.9 1.0
ND1 A:HIS206 4.4 12.6 1.0
CE1 A:HIS257 4.7 10.7 1.0
O A:HOH931 4.7 26.1 1.0
O A:HOH933 4.8 22.8 1.0
CG1 A:VAL256 4.9 9.9 1.0
CD2 A:HIS257 4.9 10.9 1.0
CB A:ASP306 5.0 10.3 0.5

Reference:

A.M.Goble, R.Toro, X.Li, A.Ornelas, H.Fan, S.Eswaramoorthy, Y.Patskovsky, B.Hillerich, R.Seidel, A.Sali, B.K.Shoichet, S.C.Almo, S.Swaminathan, M.E.Tanner, F.M.Raushel. Deamination of 6-Aminodeoxyfutalosine in Menaquinone Biosynthesis By Distantly Related Enzymes. Biochemistry V. 52 6525 2013.
ISSN: ISSN 0006-2960
PubMed: 23972005
DOI: 10.1021/BI400750A
Page generated: Mon Aug 5 06:41:02 2024

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