5L8K
Aurora-A kinase domain in complex with vNAR-D01 (crystal form 2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000212 | biological_process | meiotic spindle organization |
| A | 0000226 | biological_process | microtubule cytoskeleton organization |
| A | 0000278 | biological_process | mitotic cell cycle |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007052 | biological_process | mitotic spindle organization |
| A | 0007098 | biological_process | centrosome cycle |
| A | 0007100 | biological_process | mitotic centrosome separation |
| A | 0051321 | biological_process | meiotic cell cycle |
| B | 0002250 | biological_process | adaptive immune response |
| B | 0002376 | biological_process | immune system process |
| B | 0042101 | cellular_component | T cell receptor complex |
| B | 0042605 | molecular_function | peptide antigen binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue ADP A 501 |
| Chain | Residue |
| A | GLY140 |
| A | LEU263 |
| A | HOH624 |
| A | HOH632 |
| A | HOH651 |
| A | HOH687 |
| A | HOH719 |
| A | HOH722 |
| A | GLY142 |
| A | LYS143 |
| A | VAL147 |
| A | ALA160 |
| A | LYS162 |
| A | LEU194 |
| A | GLU211 |
| A | ALA213 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | HIS248 |
| A | MET373 |
| A | LEU374 |
| A | HOH605 |
| A | HOH629 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | LYS153 |
| A | PRO349 |
| A | ASP350 |
| A | PHE351 |
| A | HOH627 |
| A | HOH640 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | TYR246 |
| A | LYS250 |
| B | HOH333 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | SER266 |
| A | LYS339 |
| A | ARG343 |
| A | HOH608 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | GLN127 |
| A | HOH634 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | VAL163 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | HIS187 |
| B | GLU47 |
| B | LYS85 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | ARG251 |
| B | ARG55 |
| B | TYR56 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | ARG232 |
| A | THR235 |
| A | SER388 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 511 |
| Chain | Residue |
| A | ARG255 |
| A | SER278 |
| A | VAL279 |
| A | SER283 |
| A | HIS306 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 512 |
| Chain | Residue |
| A | ARG126 |
| A | GLN127 |
| A | HOH615 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 201 |
| Chain | Residue |
| B | MET1 |
| B | ALA2 |
| B | HOH307 |
| B | HOH328 |
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 |
