4MHN
Crystal structure of a glutaminyl cyclase from Ixodes scapularis
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 400 |
Chain | Residue |
A | ASP144 |
A | GLU184 |
A | HIS322 |
A | HOH827 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q16769 |
Chain | Residue | Details |
A | GLU183 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:24598748 |
Chain | Residue | Details |
A | ASP238 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24598748, ECO:0007744|PDB:4MHN, ECO:0007744|PDB:4MHY |
Chain | Residue | Details |
A | ASP144 | |
A | GLU184 | |
A | HIS322 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN57 | |
A | ASN288 |