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Manganese in PDB 1ejj: Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate

Enzymatic activity of Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate

All present enzymatic activity of Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate:
5.4.2.1;

Protein crystallography data

The structure of Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate, PDB code: 1ejj was solved by M.J.Jedrzejas, M.Chander, P.Setlow, G.Krishnasamy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 58.486, 206.293, 125.134, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 24.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate (pdb code 1ejj). 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 Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate, PDB code: 1ejj:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1ejj

Go back to Manganese Binding Sites List in 1ejj
Manganese binding site 1 out of 2 in the Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn701

b:39.8
occ:1.00
OD1 A:ASP403 2.0 44.0 1.0
NE2 A:HIS407 2.1 39.1 1.0
NE2 A:HIS462 2.2 44.9 1.0
O2P A:3PG601 2.3 59.7 1.0
O1P A:3PG601 2.6 57.5 1.0
CG A:ASP403 2.6 45.5 1.0
OD2 A:ASP403 2.6 44.3 1.0
P A:3PG601 3.0 55.7 1.0
CD2 A:HIS407 3.0 38.7 1.0
CE1 A:HIS407 3.1 38.5 1.0
CD2 A:HIS462 3.1 46.5 1.0
CE1 A:HIS462 3.3 44.7 1.0
O A:HOH1017 3.7 49.6 1.0
C3 A:3PG601 3.8 57.5 1.0
ND2 A:ASN447 3.8 40.4 1.0
CE1 A:HIS445 3.9 42.8 1.0
O4P A:3PG601 3.9 53.5 1.0
CB A:ASP403 4.0 42.9 1.0
CG A:HIS407 4.1 41.8 1.0
ND1 A:HIS407 4.1 42.1 1.0
O3P A:3PG601 4.2 56.9 1.0
NE2 A:HIS445 4.3 42.7 1.0
CG A:HIS462 4.3 44.9 1.0
ND1 A:HIS462 4.3 45.5 1.0
NZ A:LYS336 4.4 37.1 1.0
O A:ASP403 4.6 42.5 1.0
C2 A:3PG601 4.6 59.1 1.0
MN A:MN801 4.8 41.0 1.0
C A:ASP403 4.8 42.9 1.0
CA A:ASP403 4.8 43.9 1.0
OD1 A:ASP12 4.8 54.2 1.0
O1 A:3PG601 4.9 60.1 1.0
CG A:ASN447 5.0 40.5 1.0

Manganese binding site 2 out of 2 in 1ejj

Go back to Manganese Binding Sites List in 1ejj
Manganese binding site 2 out of 2 in the Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structural Analysis of Phosphoglycerate Mutase Cocrystallized with 3-Phosphoglycerate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn801

b:41.0
occ:1.00
OD1 A:ASP444 2.1 43.7 1.0
OG A:SER62 2.1 53.6 1.0
OD1 A:ASP12 2.2 54.2 1.0
NE2 A:HIS445 2.2 42.7 1.0
OD2 A:ASP12 2.7 56.1 1.0
CG A:ASP12 2.7 54.0 1.0
CG A:ASP444 2.9 44.6 1.0
CD2 A:HIS445 3.0 44.1 1.0
OD2 A:ASP444 3.0 43.4 1.0
O2P A:3PG601 3.1 59.7 1.0
CE1 A:HIS445 3.2 42.8 1.0
CB A:SER62 3.3 50.0 1.0
CA A:SER62 3.4 47.3 1.0
N A:SER62 3.5 44.9 1.0
NZ A:LYS336 3.7 37.1 1.0
CB A:ASP12 4.1 49.6 1.0
CG A:HIS445 4.1 43.8 1.0
ND1 A:HIS445 4.1 42.5 1.0
CB A:ASP444 4.3 43.8 1.0
C A:ASN61 4.3 43.3 1.0
P A:3PG601 4.4 55.7 1.0
CG A:ASP403 4.4 45.5 1.0
CE A:LYS336 4.4 43.5 1.0
N A:GLY13 4.4 49.8 1.0
CE1 A:HIS66 4.5 50.8 1.0
OD1 A:ASP403 4.5 44.0 1.0
CA A:ASP12 4.5 48.5 1.0
O4P A:3PG601 4.6 53.5 1.0
OD2 A:ASP403 4.6 44.3 1.0
CB A:ASP403 4.7 42.9 1.0
C A:ASP12 4.7 49.9 1.0
MN A:MN701 4.8 39.8 1.0
CD A:LYS336 4.8 43.0 1.0
ND1 A:HIS66 4.8 48.5 1.0
O A:ASN61 4.9 43.9 1.0
C A:SER62 4.9 47.6 1.0

Reference:

M.J.Jedrzejas, M.Chander, P.Setlow, G.Krishnasamy. Structure and Mechanism of Action of A Novel Phosphoglycerate Mutase From Bacillus Stearothermophilus. Embo J. V. 19 1419 2000.
ISSN: ISSN 0261-4189
PubMed: 10747010
DOI: 10.1093/EMBOJ/19.7.1419
Page generated: Tue Dec 15 03:47:22 2020

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