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2BMC

Aurora-2 T287D T288D complexed with PHA-680632

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
B0000212biological_processmeiotic spindle organization
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007052biological_processmitotic spindle organization
B0007098biological_processcentrosome cycle
B0007100biological_processmitotic centrosome separation
B0051321biological_processmeiotic cell cycle
C0000212biological_processmeiotic spindle organization
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0007052biological_processmitotic spindle organization
C0007098biological_processcentrosome cycle
C0007100biological_processmitotic centrosome separation
C0051321biological_processmeiotic cell cycle
D0000212biological_processmeiotic spindle organization
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
D0007052biological_processmitotic spindle organization
D0007098biological_processcentrosome cycle
D0007100biological_processmitotic centrosome separation
D0051321biological_processmeiotic cell cycle
E0000212biological_processmeiotic spindle organization
E0000226biological_processmicrotubule cytoskeleton organization
E0000278biological_processmitotic cell cycle
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
E0007052biological_processmitotic spindle organization
E0007098biological_processcentrosome cycle
E0007100biological_processmitotic centrosome separation
E0051321biological_processmeiotic cell cycle
F0000212biological_processmeiotic spindle organization
F0000226biological_processmicrotubule cytoskeleton organization
F0000278biological_processmitotic cell cycle
F0004672molecular_functionprotein kinase activity
F0005524molecular_functionATP binding
F0006468biological_processprotein phosphorylation
F0007052biological_processmitotic spindle organization
F0007098biological_processcentrosome cycle
F0007100biological_processmitotic centrosome separation
F0051321biological_processmeiotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE MPY A1395
ChainResidue
AGLY140
APRO214
AGLY216
AGLU260
AASN261
ALEU263
BSER266
BALA267
BGLY268
ALYS141
AGLY142
AVAL147
AALA160
ALYS162
AGLU211
ATYR212
AALA213

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MPY B1395
ChainResidue
BGLY140
BLYS141
BVAL147
BALA160
BLYS162
BGLU211
BTYR212
BALA213
BPRO214
BGLY216
BLYS224
BGLU260
BASN261
BLEU263

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MPY C1394
ChainResidue
CGLY140
CLYS141
CGLY142
CVAL147
CALA160
CLYS162
CLEU194
CGLU211
CTYR212
CALA213
CPRO214
CGLY216
CGLU260
CASN261
CLEU263

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MPY D1395
ChainResidue
CLEU215
DGLY140
DLYS141
DVAL147
DALA160
DLYS162
DGLU211
DTYR212
DALA213
DPRO214
DGLY216
DTHR217
DGLU260
DASN261
DLEU263

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MPY E1395
ChainResidue
EGLY140
ELYS141
EGLY142
EVAL147
EALA160
ELYS162
EGLU211
ETYR212
EALA213
EPRO214
EGLY216
EGLU260
EASN261
ELEU263

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MPY F1395
ChainResidue
ESER266
FLEU139
FGLY140
FVAL147
FALA160
FLYS162
FGLU211
FTYR212
FALA213
FPRO214
FGLU260
FASN261
FLEU263

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 Residues6
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 Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27837025","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G1X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DLYS258
DASP256

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ELYS258
EASP256

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FLYS258
FASP256

site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR292
ALYS258
AASP256

site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR292
BLYS258
BASP256

site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CTHR292
CLYS258
CASP256

site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DTHR292
DLYS258
DASP256

site_idCSA17
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ETHR292
ELYS258
EASP256

site_idCSA18
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FTHR292
FLYS258
FASP256

site_idCSA19
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS258
AASN261
AASP256

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP256
BGLU260

site_idCSA20
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS258
BASN261
BASP256

site_idCSA21
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS258
CASN261
CASP256

site_idCSA22
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DLYS258
DASN261
DASP256

site_idCSA23
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ELYS258
EASN261
EASP256

site_idCSA24
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FLYS258
FASN261
FASP256

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP256
CGLU260

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP256
DGLU260

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASP256
EGLU260

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FASP256
FGLU260

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS258
AASP256

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS258
BASP256

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS258
CASP256

239803

PDB entries from 2025-08-06

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