6R8N
STRUCTURE DETERMINATION OF THE TETRAHEDRAL AMINOPEPTIDASE TET2 FROM P. HORIKOSHII BY USE OF COMBINED SOLID-STATE NMR, SOLUTION-STATE NMR AND EM DATA 4.1 A, FOLLOWED BY REAL_SPACE_REFINEMENT AT 4.1 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004177 | molecular_function | aminopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004177 | molecular_function | aminopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004177 | molecular_function | aminopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0008237 | molecular_function | metallopeptidase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004177 | molecular_function | aminopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| F | 0008237 | molecular_function | metallopeptidase activity |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0004177 | molecular_function | aminopeptidase activity |
| G | 0006508 | biological_process | proteolysis |
| G | 0008237 | molecular_function | metallopeptidase activity |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0004177 | molecular_function | aminopeptidase activity |
| H | 0006508 | biological_process | proteolysis |
| H | 0008237 | molecular_function | metallopeptidase activity |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0004177 | molecular_function | aminopeptidase activity |
| I | 0006508 | biological_process | proteolysis |
| I | 0008237 | molecular_function | metallopeptidase activity |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0004177 | molecular_function | aminopeptidase activity |
| J | 0006508 | biological_process | proteolysis |
| J | 0008237 | molecular_function | metallopeptidase activity |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0004177 | molecular_function | aminopeptidase activity |
| K | 0006508 | biological_process | proteolysis |
| K | 0008237 | molecular_function | metallopeptidase activity |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0004177 | molecular_function | aminopeptidase activity |
| L | 0006508 | biological_process | proteolysis |
| L | 0008237 | molecular_function | metallopeptidase activity |
| L | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1001 |
| Chain | Residue |
| A | HIS68 |
| A | ASP182 |
| A | GLU213 |
| A | VAL236 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 1001 |
| Chain | Residue |
| B | HIS68 |
| B | ASP182 |
| B | GLU213 |
| B | VAL236 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 1001 |
| Chain | Residue |
| C | ASP182 |
| C | GLU213 |
| C | VAL236 |
| C | HIS68 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 1001 |
| Chain | Residue |
| D | HIS68 |
| D | ASP182 |
| D | GLU213 |
| D | VAL236 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN E 1001 |
| Chain | Residue |
| E | HIS68 |
| E | ASP182 |
| E | GLU213 |
| E | VAL236 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN F 1001 |
| Chain | Residue |
| F | HIS68 |
| F | ASP182 |
| F | GLU213 |
| F | VAL236 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN G 1001 |
| Chain | Residue |
| G | HIS68 |
| G | ASP182 |
| G | GLU213 |
| G | VAL236 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN H 1001 |
| Chain | Residue |
| H | HIS68 |
| H | ASP182 |
| H | GLU213 |
| H | VAL236 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN I 1001 |
| Chain | Residue |
| I | HIS68 |
| I | ASP182 |
| I | GLU213 |
| I | VAL236 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN J 1001 |
| Chain | Residue |
| J | HIS68 |
| J | ASP182 |
| J | GLU213 |
| J | VAL236 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN K 1001 |
| Chain | Residue |
| K | HIS68 |
| K | ASP182 |
| K | GLU213 |
| K | VAL236 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN L 1001 |
| Chain | Residue |
| L | HIS68 |
| L | ASP182 |
| L | GLU213 |
| L | VAL236 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15375159, ECO:0000269|PubMed:15713475 |
| Chain | Residue | Details |
| A | GLU212 | |
| J | GLU212 | |
| K | GLU212 | |
| L | GLU212 | |
| B | GLU212 | |
| C | GLU212 | |
| D | GLU212 | |
| E | GLU212 | |
| F | GLU212 | |
| G | GLU212 | |
| H | GLU212 | |
| I | GLU212 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 60 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS68 | |
| B | HIS323 | |
| C | HIS68 | |
| C | ASP182 | |
| C | GLU213 | |
| C | ASP235 | |
| C | HIS323 | |
| D | HIS68 | |
| D | ASP182 | |
| D | GLU213 | |
| D | ASP235 | |
| A | ASP182 | |
| D | HIS323 | |
| E | HIS68 | |
| E | ASP182 | |
| E | GLU213 | |
| E | ASP235 | |
| E | HIS323 | |
| F | HIS68 | |
| F | ASP182 | |
| F | GLU213 | |
| F | ASP235 | |
| A | GLU213 | |
| F | HIS323 | |
| G | HIS68 | |
| G | ASP182 | |
| G | GLU213 | |
| G | ASP235 | |
| G | HIS323 | |
| H | HIS68 | |
| H | ASP182 | |
| H | GLU213 | |
| H | ASP235 | |
| A | ASP235 | |
| H | HIS323 | |
| I | HIS68 | |
| I | ASP182 | |
| I | GLU213 | |
| I | ASP235 | |
| I | HIS323 | |
| J | HIS68 | |
| J | ASP182 | |
| J | GLU213 | |
| J | ASP235 | |
| A | HIS323 | |
| J | HIS323 | |
| K | HIS68 | |
| K | ASP182 | |
| K | GLU213 | |
| K | ASP235 | |
| K | HIS323 | |
| L | HIS68 | |
| L | ASP182 | |
| L | GLU213 | |
| L | ASP235 | |
| B | HIS68 | |
| L | HIS323 | |
| B | ASP182 | |
| B | GLU213 | |
| B | ASP235 |
