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2C6D

Aurora A kinase activated mutant (T287D) in complex with ADPNP

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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A1390
ChainResidue
ATYR211
ASER265
ALYS338
AARG342
AGLU344
AHOH2052
AHOH2152
AHOH2153

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ANP A1391
ChainResidue
AVAL146
AALA159
ALYS161
ALEU193
AGLU210
ATYR211
AALA212
ATHR216
AGLU259
AASN260
ALEU262
AALA272
ASER277
AVAL278
AHOH2154
AHOH2155
AHOH2156
ALEU138

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1389
ChainResidue
AHIS247
AGLU307
AMET372
ALEU373
AARG374

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK
ChainResidueDetails
ALEU138-LYS161

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL
ChainResidueDetails
AVAL251-LEU263

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337
ChainResidueDetails
AASP255

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
ChainResidueDetails
ALYS142
ALYS161
AGLU210
AGLU259
AASP273

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197
ChainResidueDetails
ATHR286

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:26246606
ChainResidueDetails
AASP287

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726
ChainResidueDetails
ASER341

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS257

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLU259
AASP255

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS257
AASP255

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR291
ALYS257
AASP255

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS257
AASP255
AASN260

226707

PDB entries from 2024-10-30

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