4YU9
Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016603 | molecular_function | glutaminyl-peptide cyclotransferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0017186 | biological_process | peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase |
| A | 0035580 | cellular_component | specific granule lumen |
| A | 0036211 | biological_process | protein modification process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1904724 | cellular_component | tertiary granule lumen |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016603 | molecular_function | glutaminyl-peptide cyclotransferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0017186 | biological_process | peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase |
| B | 0035580 | cellular_component | specific granule lumen |
| B | 0036211 | biological_process | protein modification process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1904724 | cellular_component | tertiary granule lumen |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016603 | molecular_function | glutaminyl-peptide cyclotransferase activity |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0017186 | biological_process | peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase |
| C | 0035580 | cellular_component | specific granule lumen |
| C | 0036211 | biological_process | protein modification process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 1904724 | cellular_component | tertiary granule lumen |
| C | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | ASP159 |
| A | GLU202 |
| A | HIS330 |
| A | HOH816 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | HOH592 |
| A | HOH615 |
| A | HOH763 |
| B | ARG217 |
| B | ARG312 |
| A | ARG312 |
| A | ARG313 |
| A | SO4403 |
| A | HOH572 |
| A | HOH582 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG217 |
| A | ARG312 |
| A | SO4402 |
| A | HOH576 |
| A | HOH582 |
| A | HOH589 |
| A | HOH715 |
| B | ARG312 |
| B | ARG313 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | LEU238 |
| A | HIS239 |
| A | ARG313 |
| A | GLY314 |
| A | HOH667 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | SER34 |
| A | TRP36 |
| A | ALA232 |
| A | ARG233 |
| A | THR235 |
| A | HOH765 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | SER51 |
| A | ALA52 |
| A | GLN55 |
| A | HOH503 |
| B | ARG54 |
| B | LEU281 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ASP101 |
| A | LYS182 |
| A | HOH792 |
| A | HOH832 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | ASN128 |
| A | LEU181 |
| A | ASP190 |
| A | LEU191 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | ASN41 |
| A | ARG266 |
| A | HOH514 |
| A | HOH524 |
| A | HOH638 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | ASP159 |
| B | GLU202 |
| B | HIS330 |
| B | HOH812 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | HIS239 |
| B | ARG313 |
| B | GLY314 |
| B | VAL315 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | GLU269 |
| B | GLN272 |
| B | ALA273 |
| B | EDO404 |
| B | HOH777 |
| C | ASN296 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | GLN272 |
| B | ALA273 |
| B | EDO403 |
| B | HOH699 |
| B | HOH778 |
| B | HOH779 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | THR126 |
| B | PRO129 |
| B | HIS134 |
| B | GLN194 |
| B | HIS228 |
| B | GLN237 |
| B | HOH640 |
| B | HOH676 |
| B | HOH686 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | ASN49 |
| B | HOH739 |
| B | HOH751 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 401 |
| Chain | Residue |
| C | ASP159 |
| C | GLU202 |
| C | HIS330 |
| C | HOH790 |
| site_id | AD8 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 C 402 |
| Chain | Residue |
| C | ARG217 |
| C | ARG312 |
| C | ARG312 |
| C | ARG313 |
| C | HOH501 |
| C | HOH501 |
| C | HOH512 |
| C | HOH517 |
| C | HOH520 |
| C | HOH575 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 403 |
| Chain | Residue |
| C | TYR299 |
| C | SER323 |
| C | PRO324 |
| C | PHE325 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 404 |
| Chain | Residue |
| C | ARG152 |
| C | MET332 |
| C | ASP333 |
| site_id | AE2 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 405 |
| Chain | Residue |
| C | THR126 |
| C | PRO129 |
| C | HIS134 |
| C | GLN194 |
| C | GLN237 |
| C | HOH624 |
| C | HOH692 |
| C | HOH699 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 406 |
| Chain | Residue |
| C | ALA173 |
| C | LEU174 |
| C | ASP175 |
| C | LYS176 |
| C | LYS177 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:18072935 |
| Chain | Residue | Details |
| A | GLU201 | |
| A | ASP248 | |
| B | GLU201 | |
| B | ASP248 | |
| C | GLU201 | |
| C | ASP248 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935, ECO:0000269|PubMed:21288892, ECO:0000269|PubMed:21671571, ECO:0007744|PDB:2AFM, ECO:0007744|PDB:2AFO, ECO:0007744|PDB:2AFS, ECO:0007744|PDB:2AFU, ECO:0007744|PDB:2AFW, ECO:0007744|PDB:2AFX, ECO:0007744|PDB:2AFZ, ECO:0007744|PDB:2ZED, ECO:0007744|PDB:2ZEE, ECO:0007744|PDB:2ZEF, ECO:0007744|PDB:2ZEG, ECO:0007744|PDB:2ZEH, ECO:0007744|PDB:2ZEL, ECO:0007744|PDB:2ZEM, ECO:0007744|PDB:2ZEN, ECO:0007744|PDB:2ZEO, ECO:0007744|PDB:2ZEP, ECO:0007744|PDB:3PBB, ECO:0007744|PDB:3PBE, ECO:0007744|PDB:3SI0, ECO:0007744|PDB:4YU9, ECO:0007744|PDB:4YWY |
| Chain | Residue | Details |
| A | ASP159 | |
| A | GLU202 | |
| A | HIS330 | |
| B | ASP159 | |
| B | GLU202 | |
| B | HIS330 | |
| C | ASP159 | |
| C | GLU202 | |
| C | HIS330 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21671571 |
| Chain | Residue | Details |
| A | ASN49 | |
| B | ASN49 | |
| C | ASN49 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN296 | |
| B | ASN296 | |
| C | ASN296 |
