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Iron in PDB 2zcf: Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771

Enzymatic activity of Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771

All present enzymatic activity of Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771:
4.2.1.84;

Protein crystallography data

The structure of Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771, PDB code: 2zcf was solved by H.Takarada, Y.Kawano, K.Hashimoto, H.Nakayama, S.Ueda, M.Yohda, N.Kamiya, N.Dohmae, M.Maeda, M.Odaka, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.43
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 114.838, 60.554, 82.187, 90.00, 125.05, 90.00
R / Rfree (%) 16.9 / 21.1

Other elements in 2zcf:

The structure of Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771 (pdb code 2zcf). 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 Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771, PDB code: 2zcf:

Iron binding site 1 out of 1 in 2zcf

Go back to Iron Binding Sites List in 2zcf
Iron binding site 1 out of 1 in the Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mutational Study on Alpha-GLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe206

b:5.7
occ:1.00
 O A:HOH207 2.0 9.8 1.0
N A:CSO114 2.0 5.0 1.0
N A:SER113 2.0 4.9 1.0
SG A:CSD112 2.2 4.5 1.0
SG A:CSO114 2.3 8.2 1.0
SG A:CYS109 2.3 5.0 1.0
C A:SER113 2.8 8.1 1.0
CA A:SER113 2.9 4.7 1.0
CA A:CSO114 3.0 5.1 1.0
OD1 A:CSD112 3.0 5.8 1.0
C A:CSD112 3.0 2.8 1.0
CB A:CSO114 3.1 5.2 1.0
OD A:CSO114 3.1 12.7 1.0
CB A:CSD112 3.1 4.7 1.0
OD2 A:CSD112 3.2 4.6 1.0
CB A:CYS109 3.3 7.3 1.0
CA A:CSD112 3.4 3.8 1.0
OG A:SER113 3.7 9.2 1.0
N A:CSD112 3.9 4.2 1.0
CB A:SER113 3.9 5.9 1.0
O A:SER113 4.0 5.6 1.0
O A:CSD112 4.2 4.9 1.0
C A:CSO114 4.3 4.8 1.0
O A:HOH369 4.4 32.0 1.0
O A:CSO114 4.7 5.0 1.0
CA A:CYS109 4.7 3.1 1.0
NH2 B:ARG141 4.8 6.2 1.0
C A:LEU111 4.9 4.3 1.0
O A:CYS109 4.9 5.4 1.0

Reference:

H.Takarada, Y.Kawano, K.Hashimoto, H.Nakayama, S.Ueda, M.Yohda, N.Kamiya, N.Dohmae, M.Maeda, M.Odaka. Mutational Study on ALPHAGLN90 of Fe-Type Nitrile Hydratase From Rhodococcus Sp. N771 Biosci.Biotechnol.Biochem. V. 70 881 2006.
ISSN: ISSN 0916-8451
PubMed: 16636455
DOI: 10.1271/BBB.70.881
Page generated: Sun Aug 4 05:57:47 2024

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