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

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

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
Iron	(Fe)	1 atom

The binding sites of Manganese 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 Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the O-Carbamoyltransferase Tobz in Complex with Tobramycin, Carbamoyl Phosphate and Adp, PDB code: 3vet:

Manganese 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 Manganese with other atoms in the Mn 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:Mn605 b:34.1 occ:1.00 O2A A:ADP601 2.0 29.7 1.0 O A:HOH988 2.2 26.7 1.0 O3B A:ADP601 2.2 45.5 1.0 OG A:SER530 2.2 24.7 1.0 O2P A:CP602 2.2 36.9 1.0 O A:HOH987 2.5 32.3 1.0 CB A:SER530 3.1 26.0 1.0 PA A:ADP601 3.3 33.8 1.0 PB A:ADP601 3.4 39.0 1.0 P A:CP602 3.4 36.7 1.0 O3A A:ADP601 3.6 35.9 1.0 O3P A:CP602 3.7 31.2 1.0 NZ A:LYS443 4.1 35.9 1.0 O A:CP602 4.1 31.7 1.0 N A:SER530 4.1 22.2 1.0 CA A:SER530 4.2 28.2 1.0 OD1 A:ASN532 4.2 33.0 1.0 O2B A:ADP601 4.2 38.3 1.0 O5' A:ADP601 4.2 38.6 1.0 NH2 A:ARG418 4.3 26.4 1.0 O A:PRO417 4.3 27.1 1.0 ND2 A:ASN532 4.4 31.1 1.0 O A:HOH754 4.4 39.2 1.0 O4P A:CP602 4.4 30.4 1.0 O1A A:ADP601 4.5 34.7 1.0 O1P A:CP602 4.5 32.6 1.0 O1B A:ADP601 4.5 41.1 1.0 O A:HOH838 4.6 42.1 1.0 C A:CP602 4.7 30.1 1.0 CG A:ASN532 4.7 30.1 1.0 C5' A:ADP601 4.7 33.1 1.0 OG1 A:THR529 4.9 25.7 1.0 C A:SER530 4.9 23.6 1.0 CG1 A:ILE538 4.9 25.3 1.0 O A:SER530 5.0 25.1 1.0 CD1 A:ILE538 5.0 23.1 1.0

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