6YJY
Crystal structure of human glutaminyl cyclase in complex with neurotensin 1-5
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue MES A 401 |
| Chain | Residue |
| A | LEU110 |
| A | SER111 |
| A | GLN112 |
| A | TYR117 |
| A | HOH679 |
| B | SER208 |
| B | ALA224 |
| B | ARG313 |
| B | HOH505 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | LYS144 |
| A | HIS206 |
| A | TRP207 |
| A | ASN263 |
| A | TRP329 |
| A | HIS330 |
| A | HOH504 |
| A | HOH505 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ASN128 |
| A | PRO129 |
| A | THR130 |
| A | THR183 |
| A | HOH547 |
| A | HOH702 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | SER51 |
| A | ARG54 |
| A | HOH531 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | TYR78 |
| A | ARG118 |
| A | SO4406 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 406 |
| Chain | Residue |
| A | TYR115 |
| A | ARG118 |
| A | SO4405 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 407 |
| Chain | Residue |
| A | ARG97 |
| A | ARG172 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 408 |
| Chain | Residue |
| A | ARG152 |
| A | MET332 |
| A | ASN335 |
| A | HOH703 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 409 |
| Chain | Residue |
| A | ALA232 |
| A | ARG233 |
| A | HOH528 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 410 |
| Chain | Residue |
| A | ASP159 |
| A | GLU202 |
| A | HIS330 |
| A | PCA411 |
| A | HOH597 |
| site_id | AD2 |
| Number of Residues | 15 |
| Details | binding site for residue PCA A 411 |
| Chain | Residue |
| A | ASP159 |
| A | GLU202 |
| A | TRP207 |
| A | ASP248 |
| A | ILE303 |
| A | GLN304 |
| A | ILE321 |
| A | PHE325 |
| A | TRP329 |
| A | HIS330 |
| A | ZN410 |
| A | LEU412 |
| A | TYR413 |
| A | HOH505 |
| A | HOH597 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue LEU A 412 |
| Chain | Residue |
| A | TRP207 |
| A | GLN304 |
| A | PCA411 |
| A | TYR413 |
| A | HOH505 |
| A | HOH734 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue TYR A 413 |
| Chain | Residue |
| A | PHE260 |
| A | PRO262 |
| A | TYR299 |
| A | ILE303 |
| A | SER323 |
| A | PRO324 |
| A | PHE325 |
| A | PCA411 |
| A | LEU412 |
| A | HOH711 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | LYS40 |
| B | LYS144 |
| B | LEU205 |
| B | HIS206 |
| B | TRP207 |
| B | LEU412 |
| B | LEU415 |
| B | HOH502 |
| B | HOH547 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | ARG97 |
| B | ARG172 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | ARG217 |
| B | ARG312 |
| B | HOH543 |
| B | HOH587 |
| B | HOH606 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 404 |
| Chain | Residue |
| A | ARG233 |
| B | ARG152 |
| B | MET332 |
| B | ASN335 |
| B | HOH541 |
| B | HOH607 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 405 |
| Chain | Residue |
| B | ASN128 |
| B | PRO129 |
| B | THR130 |
| B | ALA131 |
| B | THR183 |
| B | SER185 |
| B | ASP186 |
| B | LYS188 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 406 |
| Chain | Residue |
| B | HIS279 |
| B | SER288 |
| B | LEU289 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 407 |
| Chain | Residue |
| B | ARG118 |
| B | TYR145 |
| B | ASN151 |
| B | VAL153 |
| B | HOH613 |
| site_id | AE3 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 408 |
| Chain | Residue |
| B | ARG97 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 409 |
| Chain | Residue |
| B | ARG233 |
| B | HOH508 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 410 |
| Chain | Residue |
| B | ASP159 |
| B | GLU202 |
| B | HIS330 |
| B | GLN411 |
| B | PCA414 |
| site_id | AE6 |
| Number of Residues | 14 |
| Details | binding site for residue GLN B 411 |
| Chain | Residue |
| B | HIS140 |
| B | ASP159 |
| B | GLU201 |
| B | GLU202 |
| B | TRP207 |
| B | ASP248 |
| B | ILE303 |
| B | GLN304 |
| B | PHE325 |
| B | HIS330 |
| B | ZN410 |
| B | LEU412 |
| B | PCA414 |
| B | LEU415 |
| site_id | AE7 |
| Number of Residues | 8 |
| Details | binding site for residue LEU B 412 |
| Chain | Residue |
| B | TRP207 |
| B | ASN263 |
| B | SO4401 |
| B | GLN411 |
| B | TYR413 |
| B | PCA414 |
| B | LEU415 |
| B | TYR416 |
| site_id | AE8 |
| Number of Residues | 8 |
| Details | binding site for residue TYR B 413 |
| Chain | Residue |
| B | VAL302 |
| B | VAL302 |
| B | GLN304 |
| B | LEU311 |
| B | LEU412 |
| B | PCA414 |
| B | LEU415 |
| B | TYR416 |
| site_id | AE9 |
| Number of Residues | 15 |
| Details | binding site for residue PCA B 414 |
| Chain | Residue |
| B | ASP159 |
| B | GLU201 |
| B | GLU202 |
| B | TRP207 |
| B | ASP248 |
| B | ILE303 |
| B | GLN304 |
| B | TRP329 |
| B | HIS330 |
| B | ZN410 |
| B | GLN411 |
| B | LEU412 |
| B | TYR413 |
| B | LEU415 |
| B | TYR416 |
| site_id | AF1 |
| Number of Residues | 9 |
| Details | binding site for residue LEU B 415 |
| Chain | Residue |
| B | TRP207 |
| B | ASN263 |
| B | GLN304 |
| B | SO4401 |
| B | GLN411 |
| B | LEU412 |
| B | TYR413 |
| B | PCA414 |
| B | TYR416 |
| site_id | AF2 |
| Number of Residues | 8 |
| Details | binding site for residue TYR B 416 |
| Chain | Residue |
| B | VAL302 |
| B | VAL302 |
| B | GLN304 |
| B | LEU311 |
| B | LEU412 |
| B | TYR413 |
| B | PCA414 |
| B | LEU415 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:18072935 |
| Chain | Residue | Details |
| B | GLU201 | |
| B | ASP248 | |
| A | GLU201 | |
| A | ASP248 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| 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 |
| B | ASP159 | |
| B | GLU202 | |
| B | HIS330 | |
| A | ASP159 | |
| A | GLU202 | |
| A | HIS330 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21671571 |
| Chain | Residue | Details |
| B | ASN49 | |
| A | ASN49 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN296 | |
| B | ASN296 |
