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Manganese in PDB 1o99: Crystal Structure of the S62A Mutant of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate

Enzymatic activity of Crystal Structure of the S62A Mutant of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate

All present enzymatic activity of Crystal Structure of the S62A Mutant of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate:
5.4.2.1;

Protein crystallography data

The structure of Crystal Structure of the S62A Mutant of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate, PDB code: 1o99 was solved by D.J.Rigden, E.Lamani, J.E.Littlejohn, M.J.Jedrzejas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50 / 2.65
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 58.712, 207.758, 126.235, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 24.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the S62A Mutant of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate (pdb code 1o99). 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 S62A Mutant of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate, PDB code: 1o99:

Manganese binding site 1 out of 1 in 1o99

Go back to Manganese Binding Sites List in 1o99
Manganese binding site 1 out of 1 in the Crystal Structure of the S62A Mutant 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 the S62A Mutant of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn601

b:14.6
occ:1.00
 OD1 A:ASP403 2.1 9.8 1.0
NE2 A:HIS407 2.1 17.5 1.0
NE2 A:HIS462 2.2 2.9 1.0
O4P A:2PG801 2.2 29.1 1.0
OD2 A:ASP403 2.5 9.8 1.0
O1P A:2PG801 2.5 29.1 1.0
CG A:ASP403 2.6 9.8 1.0
P A:2PG801 2.9 29.1 1.0
CE1 A:HIS462 3.0 2.9 1.0
CD2 A:HIS407 3.0 17.5 1.0
CE1 A:HIS407 3.1 17.5 1.0
CD2 A:HIS462 3.3 2.9 1.0
O A:HOH2116 3.5 34.8 1.0
O3P A:2PG801 3.7 29.1 1.0
C2 A:2PG801 3.9 29.1 1.0
CE1 A:HIS445 3.9 15.2 1.0
O2P A:2PG801 4.1 29.1 1.0
ND2 A:ASN447 4.1 17.5 1.0
CB A:ASP403 4.1 9.8 1.0
NE2 A:HIS445 4.1 15.2 1.0
ND1 A:HIS462 4.1 2.9 1.0
CG A:HIS407 4.2 17.5 1.0
ND1 A:HIS407 4.2 17.5 1.0
NZ A:LYS336 4.3 19.2 1.0
C3 A:2PG801 4.3 29.1 1.0
CG A:HIS462 4.3 2.9 1.0
O1 A:2PG801 4.7 29.1 1.0
O A:HOH2106 4.7 26.7 1.0
O A:ASP403 4.7 15.4 1.0
C1 A:2PG801 4.8 29.1 1.0
CA A:ASP403 4.9 15.4 1.0
C A:ASP403 4.9 15.4 1.0

Reference:

D.J.Rigden, L.V.Mello, E.Lamani, J.E.Littlejohn, M.J.Jedrzejas. Insights Into the Catalytic Mechanism of Cofactor-Independent Phosphoglycerate Mutase From X-Ray Crystallography, Simulated Dynamics and Molecular Modeling J.Mol.Biol. V. 328 909 2003.
ISSN: ISSN 0022-2836
PubMed: 12729763
DOI: 10.1016/S0022-2836(03)00350-4
Page generated: Sat Oct 5 11:54:57 2024

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