5EK7
Structure of the autoinhibited Epha2 JMS-KD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGEFGEVYkGmlktssgkkevp......VAIK |
| Chain | Residue | Details |
| A | ILE619-LYS646 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNILV |
| Chain | Residue | Details |
| A | TYR735-VAL747 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
| Chain | Residue | Details |
| A | ASP739 | |
| B | ASP739 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ILE619 | |
| A | LYS646 | |
| B | ILE619 | |
| B | LYS646 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR588 | |
| B | TYR588 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q03145 |
| Chain | Residue | Details |
| A | TYR594 | |
| A | TYR772 | |
| B | TYR594 | |
| B | TYR772 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | TYR628 | |
| B | TYR628 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | THR647 | |
| B | THR647 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q03145 |
| Chain | Residue | Details |
| A | TYR735 | |
| B | TYR735 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | SER869 | |
| B | SER869 |
