Calcium in PDB 7v0j: Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product

The structure of Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product, PDB code: 7v0j was solved by C.A.Bingman, N.Kuch, M.E.Kutsche, A.Parker, R.W.Smith, B.G.Fox, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.17 / 2.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	92.585, 161.637, 210.439, 90, 90, 90
R / Rfree (%)	19.1 / 22.4

The binding sites of Calcium atom in the Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product (pdb code 7v0j). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product, PDB code: 7v0j:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca500 b:76.2 occ:1.00 O A:HOH603 2.1 67.7 1.0 O A:GLY228 2.2 66.7 1.0 O A:HOH607 2.3 67.7 1.0 OG A:SER227 2.4 82.5 1.0 OD1 A:ASP231 2.4 64.0 1.0 OE1 A:GLU232 2.4 59.4 1.0 OD2 A:ASP231 2.9 66.8 1.0 CG A:ASP231 3.0 62.8 1.0 O A:ASP278 3.1 65.6 1.0 CD A:GLU232 3.4 60.3 1.0 C A:GLY228 3.4 62.6 1.0 HA A:ASP279 3.6 77.9 1.0 H A:GLY228 3.6 91.7 1.0 OE2 A:GLU232 3.6 53.9 1.0 CB A:SER227 3.7 82.5 1.0 N A:GLY228 3.7 76.3 1.0 HB2 A:SER227 3.8 99.1 1.0 H A:VAL280 3.9 76.7 1.0 H A:GLU232 3.9 73.9 1.0 HG22 A:VAL280 4.0 69.4 1.0 OG A:SER225 4.0 85.7 1.0 C A:SER227 4.0 83.3 1.0 HA A:TRP229 4.1 68.5 1.0 HG A:SER225 4.1 103.0 1.0 CA A:GLY228 4.1 67.1 1.0 C A:ASP278 4.2 69.1 1.0 HB3 A:SER227 4.3 99.1 1.0 H A:ASP231 4.4 70.0 1.0 CA A:SER227 4.4 88.1 1.0 N A:TRP229 4.4 57.4 1.0 CB A:ASP231 4.5 62.4 1.0 CA A:ASP279 4.5 64.8 1.0 HG23 A:THR169 4.5 64.9 1.0 H A:SER227 4.5 109.5 1.0 N A:GLU232 4.6 61.5 1.0 O A:SER227 4.6 82.1 1.0 HB2 A:GLU232 4.6 69.6 1.0 HA3 A:GLY228 4.6 80.6 1.0 CA A:TRP229 4.7 57.0 1.0 N A:VAL280 4.7 63.8 1.0 CG A:GLU232 4.8 56.4 1.0 N A:ASP279 4.8 67.2 1.0 N A:SER227 4.8 91.2 1.0 HA2 A:GLY228 4.8 80.6 1.0 HB2 A:ASP231 4.9 74.9 1.0 CG2 A:VAL280 4.9 57.7 1.0 HG21 A:THR169 4.9 64.9 1.0 N A:ASP231 4.9 58.2 1.0 HB3 A:ASP231 4.9 74.9 1.0

Calcium binding site 2 out of 3 in the Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca500 b:75.4 occ:1.00 O B:GLY228 2.2 71.5 1.0 O B:HOH613 2.2 69.5 1.0 O B:HOH629 2.2 70.1 1.0 OE1 B:GLU232 2.4 67.5 1.0 OD1 B:ASP231 2.4 66.5 1.0 OG B:SER227 2.5 85.8 1.0 OD2 B:ASP231 3.0 62.1 1.0 CG B:ASP231 3.0 64.4 1.0 CD B:GLU232 3.3 66.7 1.0 C B:GLY228 3.3 71.1 1.0 O B:ASP278 3.4 71.5 1.0 OE2 B:GLU232 3.4 62.2 1.0 H B:GLY228 3.5 88.0 1.0 N B:GLY228 3.6 73.2 1.0 CB B:SER227 3.9 79.5 1.0 HA B:ASP279 3.9 77.8 1.0 HA B:TRP229 3.9 77.8 1.0 H B:GLU232 4.0 73.4 1.0 CA B:GLY228 4.0 79.8 1.0 C B:SER227 4.0 83.1 1.0 HG22 B:VAL280 4.1 68.5 1.0 HB2 B:SER227 4.2 95.5 1.0 H B:VAL280 4.2 67.4 1.0 O B:HOH619 4.3 72.7 1.0 HG23 B:THR169 4.3 70.6 1.0 H B:ASP231 4.3 74.0 1.0 N B:TRP229 4.3 67.5 1.0 C B:ASP278 4.5 69.7 1.0 HB3 B:SER227 4.5 95.5 1.0 CA B:SER227 4.5 88.2 1.0 HB2 B:SER225 4.5 133.5 1.0 CA B:TRP229 4.5 64.7 1.0 HA3 B:GLY228 4.5 95.9 1.0 HB2 B:GLU232 4.5 78.2 1.0 CB B:ASP231 4.5 63.3 1.0 N B:GLU232 4.6 61.0 1.0 HG21 B:THR169 4.6 70.6 1.0 H B:SER227 4.6 112.9 1.0 O B:SER227 4.6 81.9 1.0 CG B:GLU232 4.7 66.9 1.0 HA2 B:GLY228 4.8 95.9 1.0 CA B:ASP279 4.8 64.7 1.0 CG2 B:THR169 4.9 58.7 1.0 N B:ASP231 4.9 61.6 1.0 N B:SER227 4.9 94.0 1.0 HB2 B:ASP231 4.9 76.1 1.0 N B:VAL280 5.0 56.1 1.0 C B:TRP229 5.0 66.0 1.0

Calcium binding site 3 out of 3 in the Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of A Celr Catalytic Domain Active Site Mutant with Bound Cellobiose Product within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca500 b:71.0 occ:1.00 O C:GLY228 2.2 67.1 1.0 O C:HOH601 2.2 69.8 1.0 OG C:SER227 2.3 76.0 1.0 OD1 C:ASP231 2.4 64.4 1.0 O C:HOH627 2.5 68.3 1.0 OE1 C:GLU232 2.5 61.9 1.0 OD2 C:ASP231 2.9 65.1 1.0 CG C:ASP231 3.0 62.0 1.0 O C:ASP278 3.2 74.5 1.0 C C:GLY228 3.3 67.6 1.0 CD C:GLU232 3.3 58.4 1.0 H C:GLY228 3.3 93.1 1.0 OE2 C:GLU232 3.5 60.2 1.0 N C:GLY228 3.6 77.5 1.0 CB C:SER227 3.6 77.0 1.0 HA C:ASP279 3.8 74.8 1.0 HB2 C:SER227 3.9 92.5 1.0 CA C:GLY228 4.0 70.9 1.0 C C:SER227 4.0 76.8 1.0 HA C:TRP229 4.0 73.1 1.0 H C:SER227 4.1 104.0 1.0 H C:GLU232 4.1 68.1 1.0 HG22 C:VAL280 4.1 70.9 1.0 H C:VAL280 4.2 71.8 1.0 HG23 C:THR169 4.2 69.5 1.0 C C:ASP278 4.3 72.3 1.0 HB3 C:SER227 4.3 92.5 1.0 CA C:SER227 4.3 80.0 1.0 H C:ASP231 4.3 69.8 1.0 N C:TRP229 4.4 65.4 1.0 HG21 C:THR169 4.5 69.5 1.0 CB C:ASP231 4.5 58.8 1.0 N C:SER227 4.6 86.6 1.0 HA3 C:GLY228 4.6 85.1 1.0 CA C:TRP229 4.6 60.8 1.0 N C:GLU232 4.7 56.7 1.0 HB2 C:GLU232 4.7 68.5 1.0 CA C:ASP279 4.7 62.2 1.0 HA2 C:GLY228 4.7 85.1 1.0 CG C:GLU232 4.8 55.0 1.0 O C:SER227 4.8 80.9 1.0 CG2 C:THR169 4.8 57.8 1.0 HB2 C:SER225 4.8 92.8 1.0 N C:ASP279 4.9 64.8 1.0 N C:VAL280 4.9 59.8 1.0 HB2 C:ASP231 4.9 70.7 1.0 HA C:ASP278 5.0 83.5 1.0 HB3 C:ASP231 5.0 70.7 1.0 N C:ASP231 5.0 58.0 1.0

N.J.Kuch, M.E.Kutschke, A.Parker, C.A.Bingman, B.G.Fox. Contribution of Calcium Ligands in Substrate Binding and Product Release in the Acetovibrio Thermocellus Glycoside Hydrolase Family 9 Cellulase Celr. J.Biol.Chem. 04655 2023.
ISSN: ESSN 1083-351X
PubMed: 36990218
DOI: 10.1016/J.JBC.2023.104655