The binding sites of Zinc atom in the structure of The Binding Of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode Of Interaction Of A Product of Peptide Hydrolysis (pdb code 3tmn). This binding sites where shown with 5.0 Angstroms radius around Zinc atom. The 3tmn structure was solved by H.M.HOLDEN, B.W.MATTHEWS, with X-Ray Crystallography technique, brief refinement statistics is given in the table below:
Resolution (A) | 10.0-1.7 | Space group | P6122 | a (A) | 94.100 | b (A) | 94.100 | c (A) | 131.400 | alpha (°) | 90.00 | beta (°) | 90.00 | gamma (°) | 120.00 | Rfactor (%) | n/a | Rfree (%) | n/a |
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Zinc binding site 1 out of 1 in 3tmn
|  Click to enlarge |  Click to enlarge | Mono- and Stereo- picture of 5.0 Angstrom coordination sphere 1 of Zinc in the PDB 3tmn. Coordination sphere was calculated for all residues within 5.0 Angstroms distance from the central Zinc atom, shown by VdW sphere Residues shown as a stick model or VDW spheres: E: His142, E: Glu143, E: His146, E: Tyr157, E: Glu166, E: Ser169, E: His231, E: Val317, E: Hoh362, E: Hoh807, E: Hoh810, | conact list:
Atom | Atom | Distance (A) | Zn | NE2 E:His142 | 2.12 | Zn | ND1 E:His142 | 4.24 | Zn | CD2 E:His142 | 3.13 | Zn | CE1 E:His142 | 3.11 | Zn | CG E:His142 | 4.25 | Zn | OE1 E:Glu143 | 4.26 | Zn | OE2 E:Glu143 | 4.96 | Zn | CD E:Glu143 | 4.90 | Zn | NE2 E:His146 | 2.12 | Zn | ND1 E:His146 | 4.10 | Zn | CD2 E:His146 | 3.23 | Zn | CE1 E:His146 | 2.92 | Zn | CG E:His146 | 4.25 | Zn | CE2 E:Tyr157 | 4.87 | Zn | CZ E:Tyr157 | 4.75 | Zn | OH E:Tyr157 | 3.77 | Zn | OE1 E:Glu166 | 2.17 | Zn | CB E:Glu166 | 4.94 | Zn | OE2 E:Glu166 | 2.80 | Zn | CD E:Glu166 | 2.80 | Zn | CG E:Glu166 | 4.27 | Zn | CA E:Glu166 | 4.82 | Zn | CB E:Ser169 | 4.54 | Zn | OG E:Ser169 | 4.76 | Zn | NE2 E:His231 | 4.23 | Zn | CD2 E:His231 | 4.76 | Zn | O E:Val317 | 4.87 | Zn | N E:Val317 | 4.75 | Zn | C E:Val317 | 4.87 | Zn | CA E:Val317 | 4.57 | Zn | O E:Hoh362 | 4.56 | Zn | O E:Hoh807 | 4.79 | Zn | O E:Hoh810 | 2.13 |
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