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Iron in PDB 3vet: Crystal Structure of the O-Carbamoyltransferase Tobz in Complex with Tobramycin, Carbamoyl Phosphate and Adp

Protein crystallography data

The structure of Crystal Structure of the O-Carbamoyltransferase Tobz in Complex with Tobramycin, Carbamoyl Phosphate and Adp, PDB code: 3vet was solved by C.Parthier, M.T.Stubbs, S.Goerlich, F.Jaenecke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.04 / 2.20
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 98.818, 98.818, 280.908, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 20.4

Other elements in 3vet:

The structure of Crystal Structure of the O-Carbamoyltransferase Tobz in Complex with Tobramycin, Carbamoyl Phosphate and Adp also contains other interesting chemical elements:

Potassium (K) 1 atom
Manganese (Mn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the O-Carbamoyltransferase Tobz in Complex with Tobramycin, Carbamoyl Phosphate and Adp (pdb code 3vet). 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 Crystal Structure of the O-Carbamoyltransferase Tobz in Complex with Tobramycin, Carbamoyl Phosphate and Adp, PDB code: 3vet:

Iron binding site 1 out of 1 in 3vet

Go back to Iron Binding Sites List in 3vet
Iron binding site 1 out of 1 in the Crystal Structure of the O-Carbamoyltransferase Tobz in Complex with Tobramycin, Carbamoyl Phosphate and Adp


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the O-Carbamoyltransferase Tobz in Complex with Tobramycin, Carbamoyl Phosphate and Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe607

b:22.1
occ:1.00
O1A A:ADP603 2.1 28.0 1.0
NE2 A:HIS114 2.2 19.9 1.0
OD2 A:ASP338 2.2 21.5 1.0
O3B A:ADP603 2.2 34.8 1.0
NE2 A:HIS118 2.3 21.3 1.0
OD1 A:ASP137 2.4 29.9 1.0
CD2 A:HIS118 3.1 18.3 1.0
CD2 A:HIS114 3.1 24.7 1.0
CE1 A:HIS114 3.2 19.0 1.0
PA A:ADP603 3.3 24.0 1.0
CG A:ASP338 3.3 24.8 1.0
CG A:ASP137 3.3 29.8 1.0
PB A:ADP603 3.3 29.4 1.0
CE1 A:HIS118 3.3 19.7 1.0
O3A A:ADP603 3.5 26.2 1.0
CB A:ASP137 3.6 25.7 1.0
OD1 A:ASP338 3.7 30.6 1.0
O1B A:ADP603 3.8 35.1 1.0
O2A A:ADP603 4.3 19.6 1.0
ND1 A:HIS114 4.3 21.6 1.0
CG A:HIS114 4.3 20.8 1.0
CG A:HIS118 4.3 22.1 1.0
ND1 A:HIS118 4.4 21.7 1.0
O5' A:ADP603 4.4 32.1 1.0
OD2 A:ASP137 4.4 31.5 1.0
CB A:ASP338 4.6 24.7 1.0
O2B A:ADP603 4.6 36.0 1.0
N A:ASP338 4.7 21.4 1.0
CA A:ASP338 4.7 24.1 1.0
CA A:GLY309 4.8 20.8 1.0
CZ2 A:TRP71 4.8 25.4 1.0
N A:GLY310 4.9 21.8 1.0
O A:GLN139 4.9 28.0 1.0
CG1 A:VAL341 5.0 25.6 1.0

Reference:

C.Parthier, S.Gorlich, F.Jaenecke, C.Breithaupt, U.Brauer, U.Fandrich, D.Clausnitzer, U.F.Wehmeier, C.Bottcher, D.Scheel, M.T.Stubbs. The O-Carbamoyltransferase Tobz Catalyzes An Ancient Enzymatic Reaction. Angew.Chem.Int.Ed.Engl. V. 51 4046 2012.
ISSN: ISSN 1433-7851
PubMed: 22383337
DOI: 10.1002/ANIE.201108896
Page generated: Sun Aug 4 21:53:47 2024

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