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5VD9

Crystal structure of human WEE1 kinase domain in complex with RAC-IV-097, a MK1775 analogue

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 Residues14
Detailsbinding site for residue 98G A 601
ChainResidue
AILE305
AGLY382
APHE433
AASP463
AHOH718
AHOH732
APHE310
AVAL313
AALA326
AVAL360
AASN376
AGLU377
ATYR378
ACYS379

site_idAC2
Number of Residues1
Detailsbinding site for residue CL A 602
ChainResidue
AHIS494

site_idAC3
Number of Residues2
Detailsbinding site for residue EDO A 603
ChainResidue
AARG329
AHIS371

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGEFGSVFkCvkrldgci..........YAIK
ChainResidueDetails
AILE305-LYS328

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHmDIKpsNIFI
ChainResidueDetails
ALEU422-ILE434

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP426

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE305
ALYS328

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15837193
ChainResidueDetails
AASN342
AASN431
AASP463
AGLY465

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER307

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER312

227111

PDB entries from 2024-11-06

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