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5G1X

Crystal structure of Aurora-A kinase in complex with N-Myc

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
B0003700molecular_functionDNA-binding transcription factor activity
B0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP A 1390
ChainResidue
AGLY140
AALA213
ATHR217
AGLU260
AASN261
ALEU263
AASP274
AMG1391
AMG1392
AHOH2012
AHOH2017
ALYS141
AHOH2026
AHOH2111
AHOH2112
AHOH2114
AHOH2184
AHOH2188
AHOH2189
AGLY142
ALYS143
AVAL147
AALA160
ALYS162
ALEU194
AGLU211

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1391
ChainResidue
AASP274
AADP1390
AHOH2026
AHOH2036
AHOH2116
AHOH2117
AHOH2185

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1392
ChainResidue
AASN261
AASP274
AADP1390
AHOH2112
AHOH2114

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

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19668197","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"11039908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"13678582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18662907","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19668197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26246606","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues28
DetailsRegion: {"description":"Interaction with AURKA and FBXW7","evidences":[{"source":"PubMed","id":"27837025","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsMotif: {"description":"9aaTAD","evidences":[{"source":"PubMed","id":"34342803","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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