3CZU
Crystal structure of the human ephrin A2- ephrin A1 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005003 | molecular_function | ephrin receptor activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| A | 0016020 | cellular_component | membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0046875 | molecular_function | ephrin receptor binding |
| B | 0048013 | biological_process | ephrin receptor signaling pathway |
Functional Information from PROSITE/UniProt
| site_id | PS00790 |
| Number of Residues | 21 |
| Details | RECEPTOR_TYR_KIN_V_1 Receptor tyrosine kinase class V signature 1. FqDiGACVALLSVRVyykKCP |
| Chain | Residue | Details |
| A | PHE182-PRO202 |
| site_id | PS01299 |
| Number of Residues | 28 |
| Details | EPHRIN_RBD_1 Ephrin receptor-binding (ephrin RBD) domain signature. KLSeKFQrFTPftlGkEFkeghsYYyiS |
| Chain | Residue | Details |
| B | LYS103-SER130 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20505120","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23661698","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
