5OS4
Crystal structure of Aurora-A kinase in complex with an allosterically binding fragment
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | binding site for residue ADP A 401 |
| Chain | Residue |
| A | GLY140 |
| A | ALA213 |
| A | THR217 |
| A | GLU260 |
| A | ASN261 |
| A | LEU263 |
| A | ASP274 |
| A | MG402 |
| A | MG403 |
| A | HOH506 |
| A | HOH548 |
| A | GLY142 |
| A | HOH561 |
| A | HOH582 |
| A | HOH583 |
| A | HOH587 |
| A | HOH590 |
| A | HOH591 |
| A | HOH597 |
| A | LYS143 |
| A | GLY145 |
| A | VAL147 |
| A | ALA160 |
| A | LYS162 |
| A | LEU194 |
| A | GLU211 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASN261 |
| A | ASP274 |
| A | ADP401 |
| A | HOH582 |
| A | HOH591 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP274 |
| A | ADP401 |
| A | HOH506 |
| A | HOH562 |
| A | HOH583 |
| A | HOH587 |
| A | HOH625 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue A8H A 404 |
| Chain | Residue |
| A | LYS166 |
| A | GLU170 |
| A | GLU175 |
| A | TYR199 |
| A | HOH533 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | TRP128 |
| A | PHE157 |
| A | LEU159 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK |
| Chain | Residue | Details |
| A | LEU139-LYS162 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL |
| Chain | Residue | Details |
| A | VAL252-LEU264 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27837025","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G1X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19668197","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"11039908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"13678582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18662907","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19668197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26246606","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
