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6Z4Y

Crystal structure of Aurora A (STK6) in complex with macrocycle ODS2003208

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 CIT A 501
ChainResidue
ASER266
ATHR333
AGLU336
AGLU336
ALYS339
AARG340
AARG343
AHOH639

site_idAC2
Number of Residues8
Detailsbinding site for residue CIT A 502
ChainResidue
AGLU175
AHIS176
AARG180
AARG180
AHIS280
AALA281
AHOH603
AGLY173

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 503
ChainResidue
AGLN177
AGLU181
AHOH624
AHOH641

site_idAC4
Number of Residues1
Detailsbinding site for residue EDO A 504
ChainResidue
AHOH619

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 505
ChainResidue
AHIS248
ALYS309
ALEU374

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 506
ChainResidue
APRO191
AGLU269
ALYS271

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 507
ChainResidue
ALEU139
AGLY216
ATHR217
AHOH672

site_idAC8
Number of Residues14
Detailsbinding site for residue Q7Q A 508
ChainResidue
ALYS141
AGLY142
AALA160
ALYS162
ALEU208
ALEU210
AGLU211
ATYR212
AALA213
ATHR217
AASN261
ALEU263
AALA273
APHE275

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
ATHR287

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
ATHR288

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

223166

PDB entries from 2024-07-31

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