3bsqA Results
MSA highlited sevlral residues which are very highly conserves (figure 1).
The three dimentional structure was viewed using PyMol (figure 2) and these conserved residues were marked on the crystal structure. However they were not related to binding sited of Cl and Zn, but buried in the core of the protein within a pocket-like region (figure 3). All attempts to see the electrostatic nature of this pocket were unsuccessful, due to some technical probloems with PyMol.
Structural alignement of arylsulfatase K using DALI resulted several other sulfatases (figure 4).
No: Chain Z rmsd lali nres %id Description 1: 3b5q-A 73.6 0.0 464 464 100 MOLECULE: PUTATIVE SULFATASE YIDJ; 2: 3b5q-B 70.2 0.3 464 467 100 MOLECULE: PUTATIVE SULFATASE YIDJ; 3: 2qzu-A 35.1 2.5 375 465 25 MOLECULE: PUTATIVE SULFATASE YIDJ; 4: 1fsu 28.7 2.8 344 474 22 MOLECULE: N-ACETYLGALACTOSAMINE-4-SULFATASE; 5: 1n2l-A 28.4 3.0 343 483 25 MOLECULE: ARYLSULFATASE A; 6: 1n2k-A 28.3 3.2 344 482 25 MOLECULE: ARYLSULFATASE A; 7: 1e3c-P 28.2 3.2 344 481 26 MOLECULE: ARYLSULFATASE A; 8: 1e33-P 28.2 3.1 344 480 25 MOLECULE: ARYLSULFATASE A; 9: 1e2s-P 28.2 3.1 343 481 25 MOLECULE: ARYLSULFATASE A; 10: 1e1z-P 28.1 3.2 344 481 26 MOLECULE: ARYLSULFATASE A; 11: 1auk 27.9 3.1 343 481 25 MOLECULE: ARYLSULFATASE A;
Figure 4: Structurally related proteins. (No 1 and 2 are two chains of arylsulfatase K).
Protein interactions of arylsulfatase K with other proteis were vieved usig the server STRING, which revealed four major hits, depending on XXX and XXX evidence.