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6C2T

Aurora A ligand complex

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 Residues13
Detailsbinding site for residue EGJ A 401
ChainResidue
ALEU139
AALA273
AHOH512
AHOH515
AHOH539
AVAL147
AGLU211
ATYR212
AALA213
AGLY216
ATHR217
AASN261
ALEU263

site_idAC2
Number of Residues5
Detailsbinding site for residue DMS A 402
ChainResidue
ASER245
AHIS248
AMET373
ALEU374
AARG375

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 403
ChainResidue
AGLY265
ASER266
AALA267
AGLY268
AGLU269
ALYS271
AHOH513

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":"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_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
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

238582

PDB entries from 2025-07-09

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