Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6VPL

TPX2 residues 7-20 fused to Aurora A residues 116-389 with C290 disulfide bonded to compound 7-80, and in complex with AMP-PNP

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 601
ChainResidue
AASP11
BSER7
BGLU175
BHIS176
BARG179

site_idAC2
Number of Residues16
Detailsbinding site for residue ANP A 602
ChainResidue
AALA160
ALYS162
ALEU194
AGLU211
ATYR212
AALA213
ATHR217
AASP274
AMG604
AHOH734
AHOH842
BTPO288
ALEU139
AGLY140
AGLY142
ALYS143

site_idAC3
Number of Residues4
Detailsbinding site for residue MLA A 603
ChainResidue
AARG304
AHIS366
AASN367
AHOH805

site_idAC4
Number of Residues3
Detailsbinding site for residue MG A 604
ChainResidue
ALYS162
AGLU181
AANP602

site_idAC5
Number of Residues5
Detailsbinding site for residue MG A 605
ChainResidue
ASER7
AGLU175
AHIS176
AARG179
BASP11

site_idAC6
Number of Residues12
Detailsbinding site for residue R7D A 606
ChainResidue
ASER116
ALEU289
ACYS290
AMET300
AILE301
AHIS306
AHOH720
AHOH793
BARG255
BTRP277
BMET305
BTYR338

site_idAC7
Number of Residues14
Detailsbinding site for residue ANP B 601
ChainResidue
BGLY142
BLYS143
BPHE144
BVAL147
BALA160
BLYS162
BLEU194
BGLU211
BALA213
BMG604
BHOH703
BHOH704
BHOH867
BHOH881

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL B 602
ChainResidue
ATYR334
BGLY291
BTHR292
BLEU293
BASP294
BHOH707

site_idAC9
Number of Residues5
Detailsbinding site for residue MLA B 603
ChainResidue
ALYS224
BARG304
BHIS366
BASN367
BHOH789

site_idAD1
Number of Residues3
Detailsbinding site for residue MG B 604
ChainResidue
BLYS162
BGLU181
BANP601

site_idAD2
Number of Residues12
Detailsbinding site for residue R7D B 605
ChainResidue
ATRP277
AMET305
ATYR338
BLEU289
BCYS290
BLEU293
BMET300
BILE301
BHIS306
BHOH713
BHOH802
BHOH837

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337
ChainResidueDetails
AASP256
BASP256

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
ChainResidueDetails
ALYS143
BASP274
ALYS162
AGLU211
AGLU260
AASP274
BLYS143
BLYS162
BGLU211
BGLU260

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197
ChainResidueDetails
ATHR287
BTHR287

site_idSWS_FT_FI4
Number of Residues2
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
BTPO288

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726
ChainResidueDetails
ASER342
BSER342

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS258
BLYS258

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon