Manganese in PDB 6e1j: Crystal Structure of Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea

The structure of Crystal Structure of Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea, PDB code: 6e1j was solved by S.G.Lee, J.M.Jez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.75 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	71.749, 90.277, 93.975, 90.00, 107.75, 90.00
R / Rfree (%)	15.1 / 18.7

The binding sites of Manganese atom in the Crystal Structure of Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea (pdb code 6e1j). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea, PDB code: 6e1j:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Crystal Structure of Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea


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 Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn601 b:24.5 occ:1.00 O2 A:KMT603 2.0 28.9 1.0 OD2 A:ASP90 2.1 26.1 1.0 NE2 A:HIS290 2.2 22.8 1.0 NE2 A:HIS288 2.3 23.1 1.0 O A:HOH739 2.4 20.2 1.0 O5 A:KMT603 2.4 27.3 1.0 C1 A:KMT603 2.8 30.4 1.0 CE1 A:HIS290 2.9 29.6 1.0 C2 A:KMT603 3.0 34.2 1.0 CG A:ASP90 3.1 35.3 1.0 CE1 A:HIS288 3.2 24.7 1.0 CD2 A:HIS288 3.3 24.8 1.0 CD2 A:HIS290 3.3 20.8 1.0 OD1 A:ASP90 3.5 37.7 1.0 O A:HOH732 3.8 35.4 1.0 ND2 A:ASN324 4.0 18.6 1.0 O1 A:KMT603 4.0 31.4 1.0 ND1 A:HIS290 4.1 29.7 1.0 O A:HOH843 4.1 24.6 1.0 NH2 A:ARG89 4.2 31.7 1.0 ND1 A:HIS288 4.3 23.5 1.0 CG A:HIS290 4.4 24.6 1.0 CG A:HIS288 4.4 23.5 1.0 CB A:ASP90 4.4 31.0 1.0 C3 A:KMT603 4.4 38.1 1.0 C4 A:KMT603 4.8 52.6 1.0 CG A:ASN324 4.9 23.7 1.0 OD1 A:ASN324 5.0 29.3 1.0

Manganese binding site 2 out of 3 in the Crystal Structure of Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea


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 Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn602 b:40.7 occ:1.00 O A:VAL145 2.3 32.3 1.0 OE1 A:GLU147 2.4 34.0 1.0 O A:HOH757 2.7 29.5 1.0 CD A:GLU147 3.5 34.5 1.0 C A:VAL145 3.5 31.9 1.0 OE2 A:GLU147 3.8 36.6 1.0 O A:HOH891 4.2 50.6 1.0 N A:VAL145 4.3 34.9 1.0 N A:GLU147 4.4 29.6 1.0 CA A:ASP146 4.4 33.7 1.0 N A:ASP146 4.4 31.6 1.0 CA A:VAL145 4.5 36.5 1.0 O A:HOH893 4.7 42.5 1.0 CG A:GLU147 4.9 31.3 1.0 CB A:VAL145 4.9 40.1 1.0 C A:ASP146 5.0 38.1 1.0

Manganese binding site 3 out of 3 in the Crystal Structure of Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Methylthioalkylmalate Synthase (BJUMAM1.1) From Brassica Juncea within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn601 b:27.4 occ:1.00 O1 B:KMT602 2.0 29.9 1.0 OD2 B:ASP90 2.1 31.7 1.0 O B:HOH753 2.1 27.4 1.0 O5 B:KMT602 2.2 28.5 1.0 NE2 B:HIS288 2.3 28.9 1.0 NE2 B:HIS290 2.3 25.2 1.0 C1 B:KMT602 2.7 35.2 1.0 C2 B:KMT602 2.8 35.5 1.0 CE1 B:HIS290 3.1 27.5 1.0 CG B:ASP90 3.1 33.0 1.0 CE1 B:HIS288 3.2 31.4 1.0 CD2 B:HIS288 3.3 27.8 1.0 OD1 B:ASP90 3.4 45.1 1.0 CD2 B:HIS290 3.4 32.3 1.0 O2 B:KMT602 3.9 33.4 1.0 ND2 B:ASN324 4.0 25.3 1.0 ND1 B:HIS290 4.3 29.9 1.0 C3 B:KMT602 4.3 45.3 1.0 ND1 B:HIS288 4.3 28.0 1.0 NH2 B:ARG89 4.3 36.0 1.0 CG B:HIS288 4.4 28.7 1.0 CB B:ASP90 4.5 25.3 1.0 CG B:HIS290 4.5 26.0 1.0 NH1 B:ARG89 4.6 39.0 1.0 S1 B:KMT602 4.8 62.7 1.0 C4 B:KMT602 4.9 55.4 1.0 CZ B:ARG89 4.9 40.7 1.0 CG B:ASN324 4.9 30.9 1.0

R.Kumar, S.G.Lee, R.Augustine, M.Reichelt, D.G.Vassao, M.H.Palavalli, A.Allen, J.Gershenzon, J.M.Jez, N.C.Bisht. Molecular Basis of the Evolution of Methylthioalkylmalate Synthase and the Diversity of Methionine-Derived Glucosinolates. Plant Cell V. 31 1633 2019.
ISSN: ESSN 1532-298X
PubMed: 31023839
DOI: 10.1105/TPC.19.00046