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Manganese in PDB 1eqj: Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate

Enzymatic activity of Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate

All present enzymatic activity of Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate:
5.4.2.1;

Protein crystallography data

The structure of Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate, PDB code: 1eqj 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 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 58.407, 205.688, 123.706, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 25.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate (pdb code 1eqj). 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 Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate, PDB code: 1eqj:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1eqj

Go back to Manganese Binding Sites List in 1eqj
Manganese binding site 1 out of 2 in the Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate


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 Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn601

b:28.7
occ:1.00
OD1 A:ASP403 2.1 35.4 1.0
NE2 A:HIS407 2.2 31.8 1.0
NE2 A:HIS462 2.2 35.8 1.0
O4P A:2PG801 2.3 46.5 1.0
O1P A:2PG801 2.6 43.9 1.0
CG A:ASP403 2.7 38.0 1.0
OD2 A:ASP403 2.7 37.2 1.0
P A:2PG801 3.0 43.8 1.0
CD2 A:HIS407 3.0 31.9 1.0
CD2 A:HIS462 3.1 35.4 1.0
CE1 A:HIS407 3.2 30.4 1.0
CE1 A:HIS462 3.3 35.6 1.0
O A:HOH963 3.6 34.2 1.0
ND2 A:ASN447 3.6 29.6 1.0
O3P A:2PG801 3.9 46.3 1.0
CE1 A:HIS445 3.9 33.1 1.0
C2 A:2PG801 3.9 44.4 1.0
O2P A:2PG801 4.1 44.6 1.0
CB A:ASP403 4.2 35.7 1.0
CG A:HIS407 4.2 32.6 1.0
ND1 A:HIS407 4.2 31.7 1.0
CG A:HIS462 4.3 35.7 1.0
NZ A:LYS336 4.3 28.9 1.0
ND1 A:HIS462 4.3 35.4 1.0
C3 A:2PG801 4.4 45.9 1.0
NE2 A:HIS445 4.4 34.5 1.0
O1 A:2PG801 4.6 43.0 1.0
O A:ASP403 4.8 31.0 1.0
C1 A:2PG801 4.8 44.9 1.0
CG A:ASN447 4.8 30.2 1.0
OG A:SER62 4.9 36.8 1.0
O A:HOH929 4.9 32.6 1.0
MN A:MN701 4.9 32.7 1.0
C A:ASP403 4.9 33.4 1.0
CA A:ASP403 4.9 34.2 1.0
OD2 A:ASP12 5.0 36.8 1.0

Manganese binding site 2 out of 2 in 1eqj

Go back to Manganese Binding Sites List in 1eqj
Manganese binding site 2 out of 2 in the Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate


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 Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn701

b:32.7
occ:1.00
OD2 A:ASP12 2.1 36.8 1.0
OD2 A:ASP444 2.2 34.2 1.0
OG A:SER62 2.3 36.8 1.0
NE2 A:HIS445 2.3 34.5 1.0
CG A:ASP12 2.8 37.3 1.0
OD1 A:ASP12 2.9 40.1 1.0
CG A:ASP444 2.9 33.8 1.0
OD1 A:ASP444 3.0 34.2 1.0
CD2 A:HIS445 3.1 32.3 1.0
CB A:SER62 3.3 36.7 1.0
CA A:SER62 3.3 35.5 1.0
O4P A:2PG801 3.3 46.5 1.0
CE1 A:HIS445 3.3 33.1 1.0
N A:SER62 3.5 35.5 1.0
NZ A:LYS336 3.7 28.9 1.0
CB A:ASP12 4.2 35.5 1.0
C A:ASN61 4.2 35.0 1.0
CG A:HIS445 4.2 31.6 1.0
CB A:ASP444 4.3 33.5 1.0
ND1 A:HIS445 4.3 32.2 1.0
CE1 A:HIS66 4.4 34.8 1.0
CE A:LYS336 4.4 32.7 1.0
P A:2PG801 4.5 43.8 1.0
N A:GLY13 4.5 37.2 1.0
CA A:ASP12 4.5 36.4 1.0
CG A:ASP403 4.5 38.0 1.0
OD1 A:ASP403 4.6 35.4 1.0
O A:ASN61 4.6 36.2 1.0
O3P A:2PG801 4.7 46.3 1.0
ND1 A:HIS66 4.7 35.1 1.0
C A:SER62 4.7 35.3 1.0
CD A:LYS336 4.8 34.4 1.0
C A:ASP12 4.8 37.6 1.0
OD2 A:ASP403 4.8 37.2 1.0
CB A:ASP403 4.9 35.7 1.0
MN A:MN601 4.9 28.7 1.0
O2P A:2PG801 4.9 44.6 1.0

Reference:

M.J.Jedrzejas, M.Chander, P.Setlow, G.Krishnasamy. Mechanism of Catalysis of the Cofactor-Independent Phosphoglycerate Mutase From Bacillus Stearothermophilus. Crystal Structure of the Complex with 2-Phosphoglycerate. J.Biol.Chem. V. 275 23146 2000.
ISSN: ISSN 0021-9258
PubMed: 10764795
DOI: 10.1074/JBC.M002544200
Page generated: Tue Dec 15 03:47:28 2020

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