5NKH
Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with Compound 3e
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue 8ZQ A 1001 |
| Chain | Residue |
| A | LYS603 |
| A | GLU696 |
| A | LEU746 |
| A | HOH1112 |
| A | HOH1213 |
| A | HOH1267 |
| A | HOH1348 |
| A | GLY620 |
| A | ALA644 |
| A | LYS646 |
| A | ILE690 |
| A | THR692 |
| A | GLU693 |
| A | TYR694 |
| A | MET695 |
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 | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
| Chain | Residue | Details |
| A | ASP739 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ILE619 | |
| A | LYS646 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | TYR628 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | THR647 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q03145 |
| Chain | Residue | Details |
| A | TYR735 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q03145 |
| Chain | Residue | Details |
| A | TYR772 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | SER869 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER892 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKB/AKT1, RPS6KA1, RPS6KA3 AND PKA => ECO:0000269|PubMed:19573808, ECO:0000269|PubMed:26158630, ECO:0000269|PubMed:27385333, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER897 |
