2GY7
Angiopoietin-2/Tie2 Complex Crystal Structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0007596 | biological_process | blood coagulation |
| B | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
Functional Information from PROSITE/UniProt
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CiCppGfmGRtC |
| Chain | Residue | Details |
| B | CYS240-CYS251 | |
| B | CYS287-CYS298 | |
| B | CYS329-CYS340 |
| site_id | PS00514 |
| Number of Residues | 13 |
| Details | FIBRINOGEN_C_1 Fibrinogen C-terminal domain signature. WWFdaCgpSnlNG |
| Chain | Residue | Details |
| A | TRP445-GLY457 |
| site_id | PS01186 |
| Number of Residues | 16 |
| Details | EGF_2 EGF-like domain signature 2. CiCppGFmgrtcekaC |
| Chain | Residue | Details |
| B | CYS240-CYS255 | |
| B | CYS287-CYS302 | |
| B | CYS329-CYS340 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15893672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16732286","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Z3U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 79 |
| Details | Domain: {"description":"Ig-like C2-type 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 42 |
| Details | Domain: {"description":"EGF-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 45 |
| Details | Domain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 40 |
| Details | Domain: {"description":"EGF-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 90 |
| Details | Domain: {"description":"Ig-like C2-type 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16732286","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
