2AFS
Crystal structure of the genetic mutant R54W of 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 | 0016740 | molecular_function | transferase 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 | 0016740 | molecular_function | transferase 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 | HOH401 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 392 |
| Chain | Residue |
| B | ASP159 |
| B | GLU202 |
| B | HIS330 |
| B | HOH402 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 395 |
| Chain | Residue |
| A | LEU205 |
| A | HIS206 |
| A | TRP207 |
| A | TRP329 |
| A | HIS330 |
| A | HOH573 |
| A | HOH584 |
| A | HOH718 |
| A | HOH770 |
| A | LYS144 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 396 |
| Chain | Residue |
| B | LYS40 |
| B | ASN41 |
| B | LYS144 |
| B | LEU205 |
| B | HIS206 |
| B | TRP207 |
| B | HOH614 |
| B | HOH740 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18072935","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16135565","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18072935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21288892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21671571","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AFM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PBE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SI0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YWY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21671571","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
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 |
