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4AGU

CRYSTAL STRUCTURE OF THE HUMAN CDKL1 KINASE DOMAIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE D15 A 500
ChainResidue
AILE10
AASP84
AHIS89
AASN131
ALEU133
AASP144
AHOH2014
AGLY11
AGLY13
AGLY16
AVAL18
AALA31
AGLU81
ATYR82
ACYS83

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE D15 B 500
ChainResidue
BGLY11
BGLY13
BGLY16
BALA31
BPHE80
BGLU81
BTYR82
BCYS83
BASP84
BHIS89
BASN131
BLEU133
BASP144

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE D15 C 500
ChainResidue
CILE10
CGLY11
CGLY13
CGLY16
CVAL18
CALA31
CGLU81
CTYR82
CCYS83
CASP84
CHIS89
CASN131
CLEU133
CASP144
CHOH2092

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGSYGVVFkCrnrdtgqiv.........AIKK
ChainResidueDetails
AILE10-LYS34

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. CiHrDVKpeNILI
ChainResidueDetails
ACYS122-ILE134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP126
BASP126
CASP126

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE10
ALYS33
BILE10
BLYS33
CILE10
CLYS33

226707

PDB entries from 2024-10-30

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