Calcium in PDB 6aw8: 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili

The structure of 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili, PDB code: 6aw8 was solved by S.Lovell, N.Mehzabeen, K.P.Battaile, Y.Deng, R.P.Hanzlik, I.Shams, J.Moskovitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.20 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	93.643, 97.531, 104.909, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21

The binding sites of Calcium atom in the 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili (pdb code 6aw8). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili, PDB code: 6aw8:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:43.7 occ:1.00 OD1 A:ASP140 2.3 39.5 1.0 OD2 A:ASP168 2.3 44.0 1.0 O A:HOH455 2.3 59.6 1.0 O A:HOH431 2.4 39.2 1.0 OD1 A:ASN169 2.4 37.1 1.0 O A:HOH462 2.8 51.8 1.0 CG A:ASP140 3.0 41.1 1.0 OD2 A:ASP140 3.1 39.6 1.0 CG A:ASN169 3.3 42.1 1.0 CG A:ASP168 3.4 40.8 1.0 ND2 A:ASN169 3.6 42.6 1.0 CB A:ASP168 4.0 40.2 1.0 NZ A:LYS143 4.3 44.9 1.0 OD1 A:ASP168 4.3 45.0 1.0 CB A:ASP140 4.5 38.6 1.0 O A:MET40 4.6 43.9 1.0 CB A:ASN169 4.7 33.2 1.0 O A:ASP140 4.7 36.9 1.0 CG2 A:VAL42 4.8 55.4 1.0 CA A:VAL42 4.9 46.3 1.0 NZ A:LYS46 4.9 52.3 1.0

Calcium binding site 2 out of 3 in the 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca301 b:41.0 occ:1.00 OD1 B:ASP140 2.3 42.8 1.0 OD2 B:ASP168 2.3 39.7 1.0 O B:HOH430 2.4 44.7 1.0 O B:HOH427 2.4 41.6 1.0 OD1 B:ASN169 2.4 39.1 1.0 O B:HOH413 2.5 38.1 1.0 OD2 B:ASP140 2.6 42.4 1.0 CG B:ASP140 2.8 44.0 1.0 CG B:ASN169 3.4 43.0 1.0 CG B:ASP168 3.4 42.2 1.0 ND2 B:ASN169 3.8 37.2 1.0 CB B:ASP168 4.0 37.9 1.0 NZ B:LYS143 4.1 47.2 1.0 CB B:ASP140 4.3 34.6 1.0 OD1 B:ASP168 4.4 39.8 1.0 O B:MET40 4.6 44.4 1.0 O B:ASP140 4.7 33.2 1.0 CB B:ASN169 4.7 39.6 1.0 O B:SAH302 4.7 51.4 1.0 CA B:VAL42 4.8 47.9 1.0 CB B:SAH302 4.9 41.5 1.0 CG2 B:VAL42 4.9 51.2 1.0 CG B:SAH302 4.9 40.4 1.0 NZ B:LYS46 4.9 45.9 1.0 CA B:ASP140 5.0 37.2 1.0

Calcium binding site 3 out of 3 in the 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of 2.25A Resolution Domain Swapped Dimer Structure of Sah Bound Catechol O-Methyltransferase (Comt) From Nannospalax Galili within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca301 b:49.5 occ:1.00 OD1 C:ASP140 2.3 49.8 1.0 OD2 C:ASP168 2.3 44.6 1.0 OD1 C:ASN169 2.4 47.7 1.0 O C:HOH414 2.5 38.8 1.0 O C:HOH431 2.6 53.4 1.0 O C:HOH425 2.8 52.5 1.0 OD2 C:ASP140 2.9 47.2 1.0 CG C:ASP140 3.0 52.1 1.0 CG C:ASN169 3.4 42.9 1.0 OE1 C:GLU198 3.4 57.2 1.0 CG C:ASP168 3.5 46.1 1.0 ND2 C:ASN169 3.8 47.0 1.0 CD C:GLU198 4.0 63.3 1.0 CB C:ASP168 4.1 41.4 1.0 NZ C:LYS143 4.1 49.5 1.0 CB C:ASP140 4.4 42.3 1.0 OE2 C:GLU198 4.5 60.5 1.0 OD1 C:ASP168 4.5 44.5 1.0 O C:MET40 4.5 44.4 1.0 O C:ASP140 4.6 49.5 1.0 CG C:GLU198 4.7 59.9 1.0 CB C:ASN169 4.8 42.6 1.0 NZ C:LYS46 4.9 62.8 1.0 CA C:VAL42 5.0 46.1 1.0 CA C:ASP140 5.0 43.9 1.0 CG2 C:VAL42 5.0 56.0 1.0

Y.Deng, S.Lovell, N.Mehzabeen, K.P.Battaile, R.P.Hanzlik, I.Shams, J.Moskovitz. Crystal Structure of the Catechol-O-Methyl Transferase (Comt) Enzyme of the Subterranean Mole Rat (Spalax) and the Effect of L136M Substitution To Be Published.