5ZE3
Crystal structure of human lysyl oxidase-like 2 (hLOXL2) in a precursor state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
Functional Information from PROSITE/UniProt
| site_id | PS00420 |
| Number of Residues | 38 |
| Details | SRCR_1 SRCR domain signature. GayigeGrvEvlkngeWGtvCddkWdlvsasvvCrelG |
| Chain | Residue | Details |
| A | GLY331-GLY368 |
| site_id | PS00926 |
| Number of Residues | 14 |
| Details | LYSYL_OXIDASE Lysyl oxidase putative copper-binding region signature. WiWHdCHrHYHSME |
| Chain | Residue | Details |
| A | TRP620-GLU633 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 198 |
| Details | Domain: {"description":"SRCR 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00196","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 218 |
| Details | Domain: {"description":"SRCR 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00196","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 406 |
| Details | Region: {"description":"Lysyl-oxidase like"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29581294","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"29581294","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"23319596","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"23319596","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29581294","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZE3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Lysine tyrosylquinone (Lys-Tyr)","evidences":[{"source":"PubMed","id":"23319596","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29581294","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
