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Iron in PDB 2zpi: Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K

Enzymatic activity of Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K

All present enzymatic activity of Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K:
4.2.1.84;

Protein crystallography data

The structure of Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K, PDB code: 2zpi was solved by K.Hashimoto, H.Suzuki, K.Taniguchi, T.Noguchi, M.Yohda, M.Odaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.49
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 114.046, 60.230, 81.480, 90.00, 125.12, 90.00
R / Rfree (%) 15.7 / 18.2

Other elements in 2zpi:

The structure of Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K (pdb code 2zpi). 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 Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K, PDB code: 2zpi:

Iron binding site 1 out of 1 in 2zpi

Go back to Iron Binding Sites List in 2zpi
Iron binding site 1 out of 1 in the Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Complex of Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, Photo-Activated For 440MIN at 293K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:6.3
occ:1.00
 N A:CSO114 2.0 6.1 1.0
N A:SER113 2.0 5.4 1.0
C A:TB0301 2.1 2.0 0.8
SG A:CSD112 2.2 5.7 1.0
SG A:CSO114 2.2 10.3 1.0
SG A:CYS109 2.3 6.3 1.0
C A:SER113 2.9 6.0 1.0
CA A:CSO114 2.9 6.8 1.0
CA A:SER113 2.9 5.6 1.0
CB A:CSO114 3.0 7.2 1.0
OD1 A:CSD112 3.1 7.4 1.0
OD A:CSO114 3.1 9.3 0.5
C A:CSD112 3.1 5.8 1.0
OD2 A:CSD112 3.1 6.0 1.0
CB A:CSD112 3.2 6.0 1.0
CB A:CYS109 3.3 5.7 1.0
CA A:CSD112 3.5 5.3 1.0
O A:HOH1604 3.5 17.8 0.5
N A:CSD112 3.8 5.8 1.0
OG A:SER113 3.9 8.0 1.0
N A:TB0301 4.0 24.8 0.8
CB A:SER113 4.0 6.1 1.0
O A:SER113 4.1 6.4 1.0
O A:CSD112 4.2 5.8 1.0
C A:CSO114 4.2 6.6 1.0
O A:CSO114 4.7 6.2 1.0
NH2 B:ARG141 4.7 6.4 1.0
CA A:CYS109 4.7 5.5 1.0
O A:CYS109 4.9 6.1 1.0
O A:THR162 4.9 9.2 1.0
C A:LEU111 4.9 4.7 1.0
O A:HOH1639 5.0 13.6 1.0

Reference:

K.Hashimoto, H.Suzuki, K.Taniguchi, T.Noguchi, M.Yohda, M.Odaka. Catalytic Mechanism of Nitrile Hydratase Proposed By Time-Resolved X-Ray Crystallography Using A Novel Substrate, Tert-Butylisonitrile J.Biol.Chem. V. 283 36617 2008.
ISSN: ISSN 0021-9258
PubMed: 18948265
DOI: 10.1074/JBC.M806577200
Page generated: Sun Aug 4 06:20:05 2024

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