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1OL5

Structure of Aurora-A 122-403, phosphorylated on Thr287, Thr288 and bound to TPX2 1-43

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A1389
ChainResidue
AASN261
AASP274
AADP1388
AHOH2073

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A1390
ChainResidue
AHOH2125
AADP1388
AHOH2026
AHOH2028
AHOH2123
AHOH2124

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A1391
ChainResidue
ASER245
AMET373
ALEU374
AARG375
AHOH2130
AHOH2131

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1392
ChainResidue
AARG220
ALYS224
AHOH2053
AHOH2132

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1393
ChainResidue
AHIS176
AARG180
AARG286
AHOH2081
AHOH2089

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A1394
ChainResidue
AHOH2104

site_idAC7
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ADP A1388
ChainResidue
AGLY140
AGLY142
AVAL147
AALA160
ALYS162
ALEU194
AGLU211
AALA213
ATHR217
AGLU260
AASN261
ALEU263
AASP274
AMG1389
AMG1390
AHOH2122
AHOH2123
AHOH2124
AHOH2126
AHOH2127
AHOH2128
AHOH2129

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337
ChainResidueDetails
AASP256

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
ChainResidueDetails
ALYS143
ALYS162
AGLU211
AGLU260
AASP274

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197
ChainResidueDetails
ATPO287

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
ATPO288

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726
ChainResidueDetails
ASER342

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS258

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP256
AGLU260

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS258
AASP256

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR292
ALYS258
AASP256

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS258
AASN261
AASP256

226707

PDB entries from 2024-10-30

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