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

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

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

Protein crystallography data

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

Resolution Low / High (Å) 10.00 / 1.75
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 95.930, 95.930, 165.810, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 22

Iron Binding Sites:

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

Iron binding site 1 out of 1 in 3dag

Go back to Iron Binding Sites List in 3dag
Iron binding site 1 out of 1 in the The Crystal Structure of [Fe]-Hydrogenase Holoenzyme (Hmd) 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 [Fe]-Hydrogenase Holoenzyme (Hmd) From Methanocaldococcus Jannaschii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe503

b:37.9
occ:0.90
 C A:CMO504 1.8 34.1 0.9
C A:CMO502 1.8 36.2 0.9
N1 A:FEG501 2.1 36.3 1.0
O A:HOH806 2.3 27.9 0.9
SG A:CYS176 2.4 31.8 0.8
SG A:CYS176 2.4 30.6 0.2
O A:HOH805 2.8 33.4 0.9
C2 A:FEG501 2.9 37.3 1.0
C6 A:FEG501 3.0 40.4 1.0
O2 A:FEG501 3.0 38.7 1.0
O A:CMO504 3.0 35.4 0.9
O A:CMO502 3.0 30.1 0.9
C7 A:FEG501 3.1 40.9 1.0
CB A:CYS176 3.5 30.7 0.2
CB A:CYS176 3.5 31.8 0.8
C3 A:FEG501 4.3 37.8 1.0
C5 A:FEG501 4.3 37.5 1.0
C8 A:FEG501 4.5 52.4 1.0
CH2 A:TRP148 4.5 30.1 1.0
CZ2 A:TRP148 4.6 29.8 1.0
CA A:CYS176 4.7 30.7 1.0
O A:CYS204 4.7 31.5 1.0
N A:CYS176 4.7 29.8 1.0
C4 A:FEG501 4.8 37.1 1.0
O28 A:FEG501 4.9 58.9 1.0
CG A:PRO202 5.0 26.5 1.0

Reference:

S.Shima, O.Pilak, S.Vogt, M.Schick, M.S.Stagni, W.Meyer-Klaucke, E.Warkentin, R.K.Thauer, U.Ermler. The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site. Science V. 321 572 2008.
ISSN: ISSN 0036-8075
PubMed: 18653896
DOI: 10.1126/SCIENCE.1158978
Page generated: Sun Dec 13 15:03:18 2020

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