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Iron in PDB 3f46: The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme From Methanocaldococcus Jannaschii

Enzymatic activity of The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme From Methanocaldococcus Jannaschii

All present enzymatic activity of The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme From Methanocaldococcus Jannaschii:
1.12.98.2;

Protein crystallography data

The structure of The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme From Methanocaldococcus Jannaschii, PDB code: 3f46 was solved by T.Hiromoto, S.Vogt, E.Warkentin, R.K.Thauer, S.Shima, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.95
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 96.350, 96.350, 166.610, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 20.5

Iron Binding Sites:

The binding sites of Iron atom in the The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme From Methanocaldococcus Jannaschii (pdb code 3f46). 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 The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme From Methanocaldococcus Jannaschii, PDB code: 3f46:

Iron binding site 1 out of 1 in 3f46

Go back to Iron Binding Sites List in 3f46
Iron binding site 1 out of 1 in the The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme From Methanocaldococcus Jannaschii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme From Methanocaldococcus Jannaschii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe360

b:29.2
occ:1.00
 C A:CMO361 1.8 28.0 1.0
C A:CMO362 1.8 32.1 1.0
C8 A:I2C359 1.9 29.0 1.0
N1 A:I2C359 2.0 29.4 1.0
O2 A:DTV363 2.0 33.5 1.0
S1 A:DTV363 2.3 32.7 1.0
C6 A:I2C359 2.8 25.8 1.0
O8 A:I2C359 2.9 28.0 1.0
O A:CMO361 2.9 30.8 1.0
C7 A:I2C359 2.9 26.8 1.0
O A:CMO362 3.0 32.8 1.0
C2 A:I2C359 3.0 30.0 1.0
C2 A:DTV363 3.0 39.6 1.0
C1 A:DTV363 3.1 37.2 1.0
O2 A:I2C359 3.2 28.6 1.0
C5 A:I2C359 4.2 25.9 1.0
C3 A:I2C359 4.3 28.6 1.0
O A:CYS204 4.3 36.8 0.6
CB A:ALA176 4.4 38.3 1.0
C3 A:DTV363 4.4 42.5 1.0
CZ2 A:TRP148 4.4 37.4 1.0
CH2 A:TRP148 4.5 36.3 1.0
C4 A:DTV363 4.8 46.5 1.0
C4 A:I2C359 4.8 28.1 1.0
O3 A:DTV363 4.8 41.4 1.0
O A:CYS204 4.9 36.5 0.4
CG A:PRO202 4.9 37.5 1.0

Reference:

T.Hiromoto, K.Ataka, O.Pilak, S.Vogt, M.S.Stagni, W.Meyer-Klaucke, E.Warkentin, R.K.Thauer, S.Shima, U.Ermler. The Crystal Structure of C176A Mutated [Fe]-Hydrogenase Suggests An Acyl-Iron Ligation in the Active Site Iron Complex. Febs Lett. V. 583 585 2009.
ISSN: ISSN 0014-5793
PubMed: 19162018
DOI: 10.1016/J.FEBSLET.2009.01.017
Page generated: Sun Aug 4 09:56:30 2024

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