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4BGQ

Crystal structure of the human CDKL5 kinase domain

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 Residues11
DetailsBINDING SITE FOR RESIDUE 38R A 1000
ChainResidue
AVAL19
AGLU139
ACYS152
ATYR24
AALA40
ALYS42
AGLU90
ATYR91
AVAL92
AASN95
AGLU98

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1001
ChainResidue
APRO231
ASER232
AGLN298
AGLN300
AHOH2098
AHOH2149

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 1002
ChainResidue
AALA283
AASP284
AGLN290

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1003
ChainResidue
AGLU93
ASER144
AHIS145
AARG301

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 1004
ChainResidue
AHIS124
AHIS127
ALYS128
ALYS190
AHOH2152

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1005
ChainResidue
AALA78
AGLY264
AASN267
AHOH2041
AHOH2123

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGEGAYGVVLkCrhketheiv.........AIKK
ChainResidueDetails
AVAL19-LYS43

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpeNLLI
ChainResidueDetails
AILE131-ILE143

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"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

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