Magnesium in PDB 3be7: Crystal Structure of Zn-Dependent Arginine Carboxypeptidase

The structure of Crystal Structure of Zn-Dependent Arginine Carboxypeptidase, PDB code: 3be7 was solved by Y.Patskovsky, U.A.Ramagopal, R.Toro, A.J.Meyer, J.Freeman, M.Iizuka, K.Bain, L.Rodgers, F.Raushel, J.M.Sauder, S.K.Burley, S.C.Almo, New Yorksgx Research Center For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	113.420, 146.583, 255.963, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 28

The binding sites of Magnesium atom in the Crystal Structure of Zn-Dependent Arginine Carboxypeptidase (pdb code 3be7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Zn-Dependent Arginine Carboxypeptidase, PDB code: 3be7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Zn-Dependent Arginine Carboxypeptidase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Zn-Dependent Arginine Carboxypeptidase within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg503 b:34.3 occ:1.00 OE2 F:GLU392 2.4 49.5 1.0 O F:HOH557 2.4 26.4 1.0 OG1 F:THR128 2.5 37.0 1.0 O F:HOH556 2.5 31.6 1.0 O F:HOH579 2.6 35.4 1.0 O F:HOH580 3.3 47.5 1.0 CD F:GLU392 3.3 51.6 1.0 CB F:THR128 3.5 29.9 1.0 CG F:GLU392 3.8 43.7 1.0 CG2 F:THR128 3.9 27.7 1.0 O F:HOH555 4.3 35.4 1.0 OE1 F:GLU392 4.3 61.5 1.0 NZ F:LYS391 4.6 36.5 1.0 OD2 F:ASP368 4.7 35.7 1.0 CA F:THR128 4.8 31.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Zn-Dependent Arginine Carboxypeptidase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Zn-Dependent Arginine Carboxypeptidase within 5.0Å range: probe atom residue distance (Å) B Occ H:Mg502 b:37.4 occ:1.00 O H:HOH577 2.4 32.7 1.0 OE2 H:GLU392 2.4 38.7 1.0 O H:HOH578 2.5 53.4 1.0 O H:HOH512 2.5 29.9 1.0 OG1 H:THR128 2.7 39.5 1.0 O H:HOH556 2.8 27.1 1.0 CD H:GLU392 3.3 44.3 1.0 CB H:THR128 3.5 32.1 1.0 CG H:GLU392 3.6 36.1 1.0 CG2 H:THR128 4.0 34.8 1.0 OD2 H:ASP368 4.1 37.7 1.0 OD1 H:ASP366 4.4 39.7 1.0 CE H:LYS391 4.4 28.7 1.0 OE1 H:GLU392 4.4 49.1 1.0 OG1 H:THR101 4.5 28.7 1.0 OD1 H:ASP368 4.7 36.5 1.0 CG H:ASP368 4.8 37.5 1.0 O H:THR100 4.8 29.0 1.0 CA H:THR128 4.9 26.0 1.0 CG H:LYS391 5.0 27.7 1.0

D.F.Xiang, Y.Patskovsky, C.Xu, A.J.Meyer, J.M.Sauder, S.K.Burley, S.C.Almo, F.M.Raushel. Functional Identification of Incorrectly Annotated Prolidases From the Amidohydrolase Superfamily of Enzymes. Biochemistry V. 48 3730 2009.
ISSN: ISSN 0006-2960
PubMed: 19281183
DOI: 10.1021/BI900111Q