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Iron in PDB 3h65: The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme in Complex with Methylenetetrahydromethanopterin

Enzymatic activity of The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme in Complex with Methylenetetrahydromethanopterin

All present enzymatic activity of The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme in Complex with Methylenetetrahydromethanopterin:
1.12.98.2;

Protein crystallography data

The structure of The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme in Complex with Methylenetetrahydromethanopterin, PDB code: 3h65 was solved by T.Hiromoto, E.Warkentin, S.Shima, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.81 / 2.15
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 97.630, 97.630, 165.750, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 20.3

Iron Binding Sites:

The binding sites of Iron atom in the The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme in Complex with Methylenetetrahydromethanopterin (pdb code 3h65). 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 in Complex with Methylenetetrahydromethanopterin, PDB code: 3h65:

Iron binding site 1 out of 1 in 3h65

Go back to Iron Binding Sites List in 3h65
Iron binding site 1 out of 1 in the The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme in Complex with Methylenetetrahydromethanopterin


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 in Complex with Methylenetetrahydromethanopterin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe360

b:38.0
occ:1.00
 C A:CMO361 1.8 33.6 1.0
C A:CMO362 1.8 43.2 1.0
C8 A:I2C359 1.9 38.3 1.0
N1 A:I2C359 2.0 37.7 1.0
O2 A:DTV363 2.0 43.6 1.0
S1 A:DTV363 2.3 40.8 1.0
O8 A:I2C359 2.8 38.3 1.0
C6 A:I2C359 2.9 34.5 1.0
O A:CMO361 2.9 36.7 1.0
C2 A:I2C359 3.0 34.7 1.0
O A:CMO362 3.0 39.4 1.0
C7 A:I2C359 3.0 36.8 1.0
O2 A:I2C359 3.2 36.3 1.0
C2 A:DTV363 3.2 47.4 1.0
C1 A:DTV363 3.3 44.7 1.0
C5 A:I2C359 4.2 35.4 1.0
C3 A:I2C359 4.3 36.2 1.0
CB A:ALA176 4.4 48.0 1.0
C3 A:DTV363 4.4 49.8 1.0
CZ2 A:TRP148 4.5 44.2 1.0
CH2 A:TRP148 4.5 44.5 1.0
O A:CYS204 4.5 47.9 1.0
C4 A:I2C359 4.8 37.0 1.0
O3 A:DTV363 4.8 48.9 1.0
C4 A:DTV363 4.8 52.5 1.0
CG A:PRO202 4.9 45.7 1.0

Reference:

T.Hiromoto, E.Warkentin, J.Moll, U.Ermler, S.Shima. The Crystal Structure of An [Fe]-Hydrogenase-Substrate Complex Reveals the Framework For H2 Activation. Angew.Chem.Int.Ed.Engl. V. 48 6457 2009.
ISSN: ISSN 1433-7851
PubMed: 19623593
DOI: 10.1002/ANIE.200902695
Page generated: Sun Dec 13 15:07:24 2020

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