3PBE
Crystal structure of the mutant W207F of human secretory 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 |
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 | HOH861 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 392 |
Chain | Residue |
B | ASP159 |
B | GLU202 |
B | HIS330 |
B | HOH867 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 395 |
Chain | Residue |
A | LEU205 |
A | HIS206 |
A | PHE207 |
A | ASN263 |
A | TRP329 |
A | HIS330 |
A | HOH574 |
A | HOH703 |
A | HOH893 |
A | LYS144 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 B 396 |
Chain | Residue |
B | LYS40 |
B | LYS144 |
B | LEU205 |
B | HIS206 |
B | PHE207 |
B | HOH603 |
B | HOH604 |
B | HOH725 |
B | HOH836 |
B | HOH846 |
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 |