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5VDK

Crystal structure of human WEE2 kinase domain in complex with MK1775

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue PO4 A 503
ChainResidue
AHIS263
ALEU266
AGLY267
AVAL272
AVAL273
ATYR275

site_idAC2
Number of Residues5
Detailsbinding site for residue PO4 A 504
ChainResidue
AGLY395
AASP396
AASP339
ALYS341
AHIS383

site_idAC3
Number of Residues16
Detailsbinding site for residues 8X7 A 501 and PO4 A 502
ChainResidue
AVAL220
AGLY221
AGLU222
ALYS241
AGLU259
AHIS263
AVAL273
AILE287
AASN289
AGLU290
ATYR291
ACYS292
AGLY295
APHE346
AASP380
ALEU381

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGVGEFGTVYkCikrldgcv..........YAIK
ChainResidueDetails
AILE218-LYS241

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. MvHlDIKpsNIFI
ChainResidueDetails
AMET335-ILE347

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsMotif: {"description":"Nuclear export signal","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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