6GBX
Crystal structure of human glutaminyl cyclase variant Y115E-Y117E in complex with SEN177
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 | S77403 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | HOH539 |
| A | HOH539 |
| A | HOH563 |
| A | HOH575 |
| A | HOH594 |
| A | ARG217 |
| A | ARG312 |
| A | ARG312 |
| A | ARG313 |
| A | HOH513 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue S77 A 403 |
| Chain | Residue |
| A | LYS144 |
| A | ASP159 |
| A | GLU201 |
| A | GLU202 |
| A | TRP207 |
| A | ASP248 |
| A | GLN304 |
| A | ASP305 |
| A | TRP329 |
| A | HIS330 |
| A | ZN401 |
| A | HOH558 |
| A | HOH581 |
| A | HOH629 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | THR126 |
| A | PRO129 |
| A | HIS134 |
| A | GLN194 |
| A | HIS228 |
| A | GLN237 |
| A | HOH501 |
| A | HOH568 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | SER323 |
| A | PRO324 |
| A | PHE325 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ASN41 |
| A | ARG266 |
| A | HOH562 |
| A | HOH605 |
| B | HOH585 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ASN128 |
| A | LEU181 |
| A | ASP190 |
| A | LEU191 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | HIS239 |
| A | ARG313 |
| A | GLY314 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | ASP159 |
| B | GLU202 |
| B | HIS330 |
| B | S77403 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | ARG217 |
| B | ARG312 |
| B | HOH501 |
| B | HOH534 |
| B | HOH596 |
| B | HOH600 |
| B | HOH612 |
| C | ARG312 |
| C | ARG313 |
| C | HOH527 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue S77 B 403 |
| Chain | Residue |
| B | LYS144 |
| B | ASP159 |
| B | GLU201 |
| B | GLU202 |
| B | TRP207 |
| B | ASP248 |
| B | GLN304 |
| B | ASP305 |
| B | TRP329 |
| B | HIS330 |
| B | ZN401 |
| B | HOH574 |
| B | HOH621 |
| B | HOH629 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | LEU238 |
| B | HIS239 |
| B | ARG313 |
| B | GLY314 |
| B | VAL315 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | ASN41 |
| B | ASN263 |
| B | ARG266 |
| B | HOH578 |
| B | HOH586 |
| B | HOH633 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | ARG270 |
| B | HOH507 |
| C | GLU290 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | HOH505 |
| B | HOH506 |
| B | HOH581 |
| B | THR126 |
| B | PRO129 |
| B | HIS134 |
| B | GLN194 |
| B | HIS228 |
| B | GLN237 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | ASN41 |
| B | TYR42 |
| B | GLN44 |
| B | ARG266 |
| B | HOH516 |
| B | HOH635 |
| C | ASN254 |
| C | PRO324 |
| C | HOH616 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 409 |
| Chain | Residue |
| B | LEU181 |
| B | ASP190 |
| B | LEU191 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 410 |
| Chain | Residue |
| B | GLN55 |
| C | SER50 |
| C | ARG54 |
| C | HOH510 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 411 |
| Chain | Residue |
| B | SER323 |
| B | PRO324 |
| B | PHE325 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 412 |
| Chain | Residue |
| B | ALA52 |
| B | GLN55 |
| B | LYS177 |
| B | LEU361 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 401 |
| Chain | Residue |
| C | ASP159 |
| C | GLU202 |
| C | HIS330 |
| C | S77403 |
| site_id | AE4 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 C 402 |
| Chain | Residue |
| B | ARG312 |
| B | ARG313 |
| C | ARG217 |
| C | ARG312 |
| C | HOH505 |
| C | HOH508 |
| C | HOH527 |
| C | HOH577 |
| C | HOH599 |
| site_id | AE5 |
| Number of Residues | 14 |
| Details | binding site for residue S77 C 403 |
| Chain | Residue |
| C | LYS144 |
| C | ASP159 |
| C | GLU201 |
| C | GLU202 |
| C | TRP207 |
| C | ASP248 |
| C | GLN304 |
| C | ASP305 |
| C | TRP329 |
| C | HIS330 |
| C | ZN401 |
| C | HOH585 |
| C | HOH588 |
| C | HOH642 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 404 |
| Chain | Residue |
| C | ASN41 |
| C | ARG266 |
| C | HOH565 |
| C | HOH567 |
| C | HOH584 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 405 |
| Chain | Residue |
| B | GLN210 |
| B | HOH509 |
| C | LEU238 |
| C | HIS239 |
| C | ARG313 |
| C | GLY314 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 406 |
| Chain | Residue |
| C | ASN128 |
| C | LEU181 |
| C | ASP190 |
| C | LEU191 |
| site_id | AE9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 407 |
| Chain | Residue |
| C | SER323 |
| C | PRO324 |
| C | PHE325 |
| site_id | AF1 |
| Number of Residues | 9 |
| Details | binding site for residue EDO C 408 |
| Chain | Residue |
| C | THR126 |
| C | PRO129 |
| C | HIS134 |
| C | GLN194 |
| C | MET223 |
| C | HIS228 |
| C | GLN237 |
| C | HOH502 |
| C | HOH528 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 409 |
| Chain | Residue |
| C | GLU105 |
| C | ILE124 |
| C | LYS222 |
| C | GLN237 |
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 |
