Manganese in PDB 1kws: Crystal Structure of BETA1,3-Glucuronyltransferase I in Complex with the Active Udp-Glcua Donor

The structure of Crystal Structure of BETA1,3-Glucuronyltransferase I in Complex with the Active Udp-Glcua Donor, PDB code: 1kws was solved by L.C.Pedersen, T.A.Darden, M.Negishi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.68 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.625, 47.978, 102.152, 90.00, 93.10, 90.00
R / Rfree (%)	18.7 / 22.3

The binding sites of Manganese atom in the Crystal Structure of BETA1,3-Glucuronyltransferase I in Complex with the Active Udp-Glcua Donor (pdb code 1kws). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of BETA1,3-Glucuronyltransferase I in Complex with the Active Udp-Glcua Donor, PDB code: 1kws:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of BETA1,3-Glucuronyltransferase I in Complex with the Active Udp-Glcua Donor


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 BETA1,3-Glucuronyltransferase I in Complex with the Active Udp-Glcua Donor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:12.6 occ:1.00 O1B A:UGA404 2.1 14.2 1.0 O A:HOH501 2.1 10.8 1.0 O1A A:UGA404 2.1 16.8 1.0 OD1 A:ASP196 2.1 9.9 1.0 O A:HOH502 2.1 6.4 1.0 OD2 A:ASP196 2.2 6.9 1.0 CG A:ASP196 2.4 4.5 1.0 PB A:UGA404 3.3 13.2 1.0 PA A:UGA404 3.4 15.5 1.0 O3A A:UGA404 3.6 14.1 1.0 O3B A:UGA404 3.8 15.3 1.0 CB A:ASP196 3.9 9.5 1.0 OD1 A:ASN197 4.0 13.1 1.0 NE2 A:HIS308 4.0 13.5 1.0 NH1 A:ARG310 4.0 39.1 1.0 O A:HOH515 4.0 7.6 1.0 CG A:ARG310 4.1 21.4 1.0 CE1 A:HIS308 4.2 14.3 1.0 O A:THR309 4.2 8.0 1.0 CB A:ASP194 4.4 8.5 1.0 O2A A:UGA404 4.5 14.9 1.0 O5D A:UGA404 4.5 14.4 1.0 OD1 A:ASP194 4.5 11.0 1.0 C5D A:UGA404 4.5 13.1 1.0 O2B A:UGA404 4.6 13.8 1.0 CD2 A:HIS308 4.7 11.8 1.0 O A:HOH510 4.7 10.2 1.0 CA A:ASP196 4.7 8.8 1.0 CG A:ASN197 4.7 11.1 1.0 N A:ASP196 4.8 7.4 1.0 CD A:ARG310 4.8 26.8 1.0 ND1 A:HIS308 4.9 13.7 1.0 C A:ASP196 4.9 10.7 1.0 N A:ASN197 4.9 10.6 1.0 CG A:ASP194 4.9 9.4 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of BETA1,3-Glucuronyltransferase I in Complex with the Active Udp-Glcua Donor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of BETA1,3-Glucuronyltransferase I in Complex with the Active Udp-Glcua Donor within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn501 b:15.7 occ:1.00 O1B B:UGA405 2.1 16.9 1.0 O B:HOH502 2.1 12.0 1.0 O B:HOH503 2.1 12.9 1.0 O1A B:UGA405 2.1 18.5 1.0 OD2 B:ASP196 2.1 10.8 1.0 OD1 B:ASP196 2.4 11.3 1.0 CG B:ASP196 2.6 12.7 1.0 PB B:UGA405 3.3 15.8 1.0 PA B:UGA405 3.4 18.9 1.0 O3A B:UGA405 3.6 16.3 1.0 O3B B:UGA405 3.7 17.6 1.0 NH1 B:ARG310 3.8 35.7 1.0 OD1 B:ASN197 4.0 9.1 1.0 O B:HOH511 4.0 10.3 1.0 CB B:ASP196 4.1 11.8 1.0 NE2 B:HIS308 4.1 14.0 1.0 CE1 B:HIS308 4.2 13.8 1.0 O B:THR309 4.3 10.2 1.0 O5D B:UGA405 4.4 18.3 1.0 CG B:ARG310 4.4 18.4 1.0 C5D B:UGA405 4.4 18.3 1.0 O2A B:UGA405 4.5 19.5 1.0 CB B:ASP194 4.5 12.2 1.0 O2B B:UGA405 4.6 17.2 1.0 OD1 B:ASP194 4.6 15.5 1.0 O B:HOH507 4.8 4.8 1.0 CD2 B:HIS308 4.8 12.6 1.0 CA B:ASP196 4.8 10.1 1.0 CG B:ASN197 4.8 9.7 1.0 N B:ASP196 4.9 8.8 1.0 ND1 B:HIS308 4.9 14.2 1.0 C B:ASP196 4.9 10.7 1.0 N B:ASN197 5.0 9.9 1.0

L.C.Pedersen, T.A.Darden, M.Negishi. Crystal Structure of Beta 1,3-Glucuronyltransferase I in Complex with Active Donor Substrate Udp-Glcua. J.Biol.Chem. V. 277 21869 2002.
ISSN: ISSN 0021-9258
PubMed: 11950836
DOI: 10.1074/JBC.M112343200