2AFZ
Crystal structure of human glutaminyl cyclase in complex with 1-vinylimidazole
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 391 |
| Chain | Residue |
| A | ASP159 |
| A | GLU202 |
| A | HIS330 |
| A | NVI381 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 392 |
| Chain | Residue |
| B | ASP159 |
| B | GLU202 |
| B | HIS330 |
| B | NVI1381 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 395 |
| Chain | Residue |
| A | HIS206 |
| A | TRP207 |
| A | ASN263 |
| A | TRP329 |
| A | HIS330 |
| A | HOH592 |
| A | HOH955 |
| A | LYS144 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 396 |
| Chain | Residue |
| B | LYS144 |
| B | LEU205 |
| B | HIS206 |
| B | TRP207 |
| B | HOH628 |
| B | HOH629 |
| B | HOH781 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NVI A 381 |
| Chain | Residue |
| A | ASP159 |
| A | GLU201 |
| A | GLU202 |
| A | ASP248 |
| A | ILE303 |
| A | GLN304 |
| A | ASP305 |
| A | ILE321 |
| A | TRP329 |
| A | HIS330 |
| A | ZN391 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NVI B 1381 |
| Chain | Residue |
| B | ASP159 |
| B | GLU201 |
| B | GLU202 |
| B | ASP248 |
| B | ILE303 |
| B | GLN304 |
| B | ASP305 |
| B | ILE321 |
| B | TRP329 |
| B | HIS330 |
| B | ZN392 |
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 |
| A | GLU201 | |
| A | ASP248 | |
| B | GLU201 | |
| B | 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 |
| A | ASP159 | |
| A | GLU202 | |
| A | HIS330 | |
| B | ASP159 | |
| B | GLU202 | |
| B | HIS330 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21671571 |
| Chain | Residue | Details |
| A | ASN49 | |
| B | 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| A | GLU201 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| B | GLU201 |
