Calcium in PDB 4w8l: Structure of GH10 From Paenibacillus Barcinonensis

All present enzymatic activity of Structure of GH10 From Paenibacillus Barcinonensis:
3.2.1.8;

The structure of Structure of GH10 From Paenibacillus Barcinonensis, PDB code: 4w8l was solved by M.A.Sainz-Polo, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.57 / 1.76
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	126.689, 126.689, 57.700, 90.00, 90.00, 120.00
R / Rfree (%)	21.8 / 25.2

The binding sites of Calcium atom in the Structure of GH10 From Paenibacillus Barcinonensis (pdb code 4w8l). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Structure of GH10 From Paenibacillus Barcinonensis, PDB code: 4w8l:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Structure of GH10 From Paenibacillus Barcinonensis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of GH10 From Paenibacillus Barcinonensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1101 b:23.9 occ:1.00 O A:HOH1394 2.2 30.0 1.0 O A:ASP504 2.2 24.1 1.0 OD1 A:ASP498 2.3 24.0 1.0 OD1 A:ASP502 2.4 25.9 1.0 OD1 A:ASP500 2.4 27.2 1.0 OD1 A:ASP507 2.4 17.0 1.0 OD2 A:ASP507 2.6 17.9 1.0 CG A:ASP507 2.8 16.7 1.0 CG A:ASP500 3.3 27.6 1.0 CG A:ASP502 3.3 26.8 1.0 C A:ASP504 3.4 23.0 1.0 CG A:ASP498 3.4 23.1 1.0 OD2 A:ASP500 3.7 28.0 1.0 OD2 A:ASP502 4.0 27.1 1.0 CA A:ASP498 4.1 21.3 1.0 N A:ASP502 4.1 27.7 1.0 N A:ASP504 4.1 25.6 1.0 CA A:ASP504 4.2 25.0 1.0 CB A:ASP498 4.2 21.8 1.0 N A:ASP500 4.3 26.1 1.0 OD2 A:ASP498 4.3 23.6 1.0 C A:ASP498 4.3 22.6 1.0 CB A:ASP507 4.3 15.5 1.0 CB A:ASP504 4.3 25.7 1.0 CB A:ASP502 4.4 26.9 1.0 N A:ASP505 4.4 21.0 1.0 N A:GLY501 4.4 28.7 1.0 N A:VAL499 4.5 22.9 1.0 CA A:ASP505 4.5 19.5 1.0 CB A:ASP500 4.6 27.0 1.0 OD2 A:ASP504 4.6 27.7 1.0 O A:HOH1389 4.6 27.6 1.0 CA A:ASP502 4.6 26.8 1.0 CA A:ASP500 4.8 27.6 1.0 N A:ASP507 4.8 15.1 1.0 N A:GLY503 4.9 25.2 1.0 C A:ASP500 4.9 28.6 1.0 C A:ASP502 4.9 25.9 1.0 O A:ASP498 4.9 23.4 1.0 CA A:ASP507 4.9 14.8 1.0

Calcium binding site 2 out of 3 in the Structure of GH10 From Paenibacillus Barcinonensis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of GH10 From Paenibacillus Barcinonensis within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1101 b:24.2 occ:1.00 O B:HOH1346 2.2 36.0 1.0 O B:ASP504 2.2 22.6 1.0 OD1 B:ASP500 2.3 28.0 1.0 OD1 B:ASP502 2.4 26.9 1.0 OD1 B:ASP507 2.5 19.5 1.0 OD1 B:ASP498 2.5 24.7 1.0 OD2 B:ASP507 2.6 20.3 1.0 CG B:ASP507 2.9 19.2 1.0 CG B:ASP500 3.3 28.3 1.0 CG B:ASP502 3.4 27.9 1.0 C B:ASP504 3.4 22.9 1.0 CG B:ASP498 3.4 24.0 1.0 OD2 B:ASP500 3.7 30.4 1.0 CA B:ASP498 4.0 23.3 1.0 OD2 B:ASP502 4.0 27.3 1.0 N B:ASP502 4.1 28.6 1.0 N B:ASP504 4.1 25.4 1.0 CB B:ASP498 4.1 23.2 1.0 CA B:ASP504 4.2 24.5 1.0 N B:ASP500 4.2 27.2 1.0 C B:ASP498 4.3 24.2 1.0 OD2 B:ASP498 4.3 24.7 1.0 N B:VAL499 4.3 24.8 1.0 CB B:ASP504 4.4 25.9 1.0 N B:GLY501 4.4 28.5 1.0 CB B:ASP507 4.4 17.8 1.0 CB B:ASP502 4.4 27.3 1.0 N B:ASP505 4.4 21.6 1.0 CA B:ASP505 4.5 20.0 1.0 CB B:ASP500 4.6 28.2 1.0 OD2 B:ASP504 4.6 28.6 1.0 CA B:ASP502 4.6 27.6 1.0 O B:HOH1309 4.7 23.8 1.0 N B:GLY503 4.7 27.1 1.0 CA B:ASP500 4.8 28.0 1.0 N B:ASP507 4.8 16.9 1.0 C B:ASP502 4.9 27.7 1.0 C B:ASP500 4.9 28.4 1.0 O B:ASP498 4.9 25.5 1.0 CG B:ASP504 4.9 27.5 1.0

Calcium binding site 3 out of 3 in the Structure of GH10 From Paenibacillus Barcinonensis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structure of GH10 From Paenibacillus Barcinonensis within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca1101 b:25.1 occ:1.00 O C:HOH1341 2.2 31.0 1.0 OD1 C:ASP502 2.3 26.4 1.0 OD1 C:ASP498 2.4 24.4 1.0 OD1 C:ASP500 2.4 25.8 1.0 OD1 C:ASP507 2.4 19.6 1.0 O C:ASP504 2.4 23.5 1.0 OD2 C:ASP507 2.6 20.6 1.0 CG C:ASP507 2.9 19.7 1.0 CG C:ASP502 3.2 27.3 1.0 CG C:ASP500 3.3 26.9 1.0 CG C:ASP498 3.4 23.2 1.0 C C:ASP504 3.5 23.2 1.0 OD2 C:ASP500 3.7 28.2 1.0 OD2 C:ASP502 3.8 27.7 1.0 N C:ASP502 4.1 28.7 1.0 CA C:ASP498 4.1 22.5 1.0 OD2 C:ASP498 4.2 23.4 1.0 N C:ASP500 4.2 25.8 1.0 N C:ASP504 4.3 25.8 1.0 CB C:ASP502 4.3 27.5 1.0 CB C:ASP498 4.3 22.5 1.0 CA C:ASP504 4.3 24.2 1.0 CB C:ASP507 4.3 18.4 1.0 CB C:ASP504 4.4 25.6 1.0 N C:GLY501 4.4 28.5 1.0 C C:ASP498 4.4 23.5 1.0 N C:VAL499 4.4 24.3 1.0 N C:ASP505 4.5 21.6 1.0 NZ C:LYS552 4.5 36.4 1.0 CB C:ASP500 4.6 26.8 1.0 CA C:ASP502 4.6 27.6 1.0 CA C:ASP505 4.6 21.1 1.0 OD2 C:ASP504 4.6 26.3 1.0 O C:HOH1280 4.6 27.5 1.0 CA C:ASP500 4.7 27.0 1.0 O C:HOH1324 4.7 29.0 1.0 N C:GLY503 4.8 26.4 1.0 N C:ASP507 4.8 17.5 1.0 C C:ASP500 4.9 27.9 1.0 C C:ASP502 4.9 27.9 1.0 CA C:ASP507 4.9 17.3 1.0 N C:SER506 5.0 19.7 1.0

M.A.Sainz-Polo, B.Gonzalez, M.Menendez, F.I.Pastor, J.Sanz-Aparicio. Exploring Multimodularity in Plant Cell Wall Deconstruction: Structural and Functional Analysis of XYN10C Containing the CBM22-1-CBM22-2 Tandem. J.Biol.Chem. V. 290 17116 2015.
ISSN: ESSN 1083-351X
PubMed: 26001782
DOI: 10.1074/JBC.M115.659300