Atomistry » Iron » PDB 2z5z-2zpg » 2zpe
Atomistry »
  Iron »
    PDB 2z5z-2zpg »
      2zpe »

Iron in PDB 2zpe: Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile

Enzymatic activity of Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile

All present enzymatic activity of Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile:
4.2.1.84;

Protein crystallography data

The structure of Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, PDB code: 2zpe 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 / 1.48
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 113.976, 60.002, 81.707, 90.00, 125.08, 90.00
R / Rfree (%) 16.5 / 19.3

Other elements in 2zpe:

The structure of Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile also contains other interesting chemical elements:

Magnesium (Mg) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile (pdb code 2zpe). 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 Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile, PDB code: 2zpe:

Iron binding site 1 out of 1 in 2zpe

Go back to Iron Binding Sites List in 2zpe
Iron binding site 1 out of 1 in the Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Nitrosylated Fe-Type Nitrile Hydratase with Tert- Butylisonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:7.2
occ:1.00
N A:CSO114 2.0 7.9 1.0
N A:NO301 2.0 11.7 1.0
N A:SER113 2.0 6.9 1.0
SG A:CSD112 2.2 7.1 1.0
SG A:CSO114 2.2 10.7 1.0
SG A:CYS109 2.4 7.4 1.0
C A:SER113 2.9 7.1 1.0
CA A:CSO114 3.0 8.3 1.0
CA A:SER113 3.0 6.8 1.0
O A:NO301 3.0 16.7 1.0
CB A:CSO114 3.1 8.9 1.0
OD1 A:CSD112 3.1 7.7 1.0
C A:CSD112 3.1 6.3 1.0
OD A:CSO114 3.1 14.2 1.0
OD2 A:CSD112 3.2 6.8 1.0
CB A:CSD112 3.2 7.0 1.0
CB A:CYS109 3.4 7.2 1.0
CA A:CSD112 3.5 6.2 1.0
OG A:SER113 3.8 9.5 1.0
N A:CSD112 3.8 6.7 1.0
CB A:SER113 4.0 7.4 1.0
O A:SER113 4.1 7.2 1.0
O A:CSD112 4.2 5.7 1.0
C A:CSO114 4.3 8.0 1.0
O A:CSO114 4.7 7.3 1.0
NH2 B:ARG141 4.7 8.5 1.0
CA A:CYS109 4.8 6.7 1.0
O A:HOH1654 4.9 16.9 1.0
O A:CYS109 5.0 6.8 1.0
O A:THR162 5.0 10.2 1.0
C A:LEU111 5.0 6.8 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 Dec 13 14:59:07 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy