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6HJJ

Crystal structure of Aurora-A L210C catalytic domain in complex with ASDO6 ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0000212biological_processmeiotic spindle organization
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007052biological_processmitotic spindle organization
A0007098biological_processcentrosome cycle
A0007100biological_processmitotic centrosome separation
A0051321biological_processmeiotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue G7T A 501
ChainResidue
ALEU139
AGLU211
AALA213
ALEU263
AALA273
APHE275
AGLY140
AALA160
ALYS162
ALEU169
AVAL174
AGLN177
ALEU178
AGLU181

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 502
ChainResidue
ATHR333
AGLU345

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 503
ChainResidue
AARG343
AHOH616

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 504
ChainResidue
AGLN335
AHOH653

site_idAC5
Number of Residues3
Detailsbinding site for residue ACT A 505
ChainResidue
ASER361
ALYS365
AHOH652

site_idAC6
Number of Residues3
Detailsbinding site for residue ACT A 506
ChainResidue
AARG151
ALYS156
AASN332

site_idAC7
Number of Residues6
Detailsbinding site for residue ACT A 507
ChainResidue
AARG220
ALYS224
AHIS366
AASN367
AHOH602
AHOH639

site_idAC8
Number of Residues3
Detailsbinding site for residue PGF A 508
ChainResidue
ALEU225
ASER226
ALYS227

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK
ChainResidueDetails
ALEU139-LYS162

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL
ChainResidueDetails
AVAL252-LEU264

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27837025","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G1X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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