Aluminium in PDB 2f90: Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4-

All present enzymatic activity of Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4-:
3.1.3.13; 5.4.2.1; 5.4.2.4;

The structure of Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4-, PDB code: 2f90 was solved by Y.Wang, L.Liu, Z.Wei, W.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.351, 71.652, 158.772, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 22.8

The structure of Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4- also contains other interesting chemical elements:

Fluorine

(F)

8 atoms

The binding sites of Aluminium atom in the Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4- (pdb code 2f90). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4-, PDB code: 2f90:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4- within 5.0Å range: probe atom residue distance (Å) B Occ A:Al400 b:14.5 occ:1.00 AL A:ALF400 0.0 14.5 1.0 F2 A:ALF400 1.8 13.7 1.0 F1 A:ALF400 1.8 14.2 1.0 F4 A:ALF400 1.8 13.6 1.0 F3 A:ALF400 1.8 14.2 1.0 O3 A:3PG408 2.0 12.1 1.0 NE2 A:HIS11 2.1 14.3 1.0 CD2 A:HIS11 3.0 14.5 1.0 C2 A:3PG408 3.1 15.1 1.0 CE1 A:HIS11 3.1 16.6 1.0 OE2 A:GLU89 3.9 12.9 1.0 NE A:ARG62 3.9 12.7 1.0 C1 A:3PG408 3.9 15.8 1.0 NH2 A:ARG62 3.9 12.7 1.0 O A:HOH588 4.0 33.6 1.0 NE A:ARG10 4.0 14.4 1.0 NH2 A:ARG10 4.1 12.8 1.0 C3 A:3PG408 4.2 13.3 1.0 CG A:HIS11 4.2 14.1 1.0 ND1 A:HIS11 4.2 15.9 1.0 ND1 A:HIS188 4.3 12.6 1.0 N A:GLY189 4.4 13.0 1.0 CZ A:ARG62 4.4 12.7 1.0 ND2 A:ASN17 4.5 15.8 1.0 CB A:HIS188 4.5 11.8 1.0 O1 A:3PG408 4.5 16.3 1.0 CZ A:ARG10 4.5 14.0 1.0 CD A:GLU89 4.6 16.5 1.0 CG A:GLU89 4.6 11.7 1.0 O2 A:3PG408 4.7 19.4 1.0 CG A:ARG10 4.9 14.2 1.0 CG A:HIS188 4.9 14.5 1.0 CA A:HIS188 4.9 12.7 1.0 CD A:ARG62 4.9 11.7 1.0

Aluminium binding site 2 out of 2 in the Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Crystal Structure of Bisphosphoglycerate Mutase in Complex with 3-Phosphoglycerate and ALF4- within 5.0Å range: probe atom residue distance (Å) B Occ B:Al401 b:16.5 occ:1.00 AL B:ALF401 0.0 16.5 1.0 F2 B:ALF401 1.8 13.2 1.0 F1 B:ALF401 1.8 16.4 1.0 F4 B:ALF401 1.8 17.0 1.0 F3 B:ALF401 1.8 15.4 1.0 O3 B:3PG409 2.0 15.4 1.0 NE2 B:HIS11 2.1 15.7 1.0 CD2 B:HIS11 3.1 15.1 1.0 CE1 B:HIS11 3.1 16.0 1.0 C2 B:3PG409 3.1 18.0 1.0 OE2 B:GLU89 3.8 11.5 1.0 NE B:ARG62 3.9 12.3 1.0 C1 B:3PG409 4.0 17.9 1.0 NE B:ARG10 4.0 11.8 1.0 NH2 B:ARG10 4.0 13.2 1.0 NH2 B:ARG62 4.1 14.0 1.0 C3 B:3PG409 4.2 17.1 1.0 ND1 B:HIS11 4.2 15.7 1.0 CG B:HIS11 4.2 14.7 1.0 ND1 B:HIS188 4.2 15.0 1.0 N B:GLY189 4.3 14.3 1.0 O B:HOH601 4.4 39.5 1.0 CB B:HIS188 4.4 14.2 1.0 ND2 B:ASN17 4.5 15.1 1.0 CZ B:ARG62 4.5 13.3 1.0 CZ B:ARG10 4.5 13.6 1.0 O2 B:3PG409 4.6 22.3 1.0 CD B:GLU89 4.6 13.8 1.0 CG B:GLU89 4.6 12.5 1.0 O1 B:3PG409 4.7 20.9 1.0 CG B:HIS188 4.8 13.8 1.0 CA B:HIS188 4.9 14.1 1.0 CG B:ARG10 4.9 13.2 1.0 CD B:ARG62 4.9 13.2 1.0 OD1 B:ASN17 5.0 18.1 1.0

Y.Wang, L.Liu, Z.Wei, Z.Cheng, Y.Lin, W.Gong. Seeing the Process of Histidine Phosphorylation in Human Bisphosphoglycerate Mutase J.Biol.Chem. V. 281 39642 2006.
ISSN: ISSN 0021-9258
PubMed: 17052986
DOI: 10.1074/JBC.M606421200