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4FG9

Crystal structure of human calcium/calmodulin-dependent protein kinase I 1-320 in complex with ATP

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
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 401
ChainResidue
AGLY27
AVAL98
AGLU102
AASP141
ALYS143
AGLU145
AASN146
ALEU148
AASP162
AHOH563
ATHR28
AGLY29
AALA30
ASER32
AVAL34
AALA47
ALYS49
AGLN96

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ATP B 401
ChainResidue
BLEU26
BGLY27
BGLY29
BALA30
BSER32
BVAL34
BALA47
BLYS49
BVAL79
BGLN96
BVAL98
BGLU102
BLYS143
BASN146
BLEU148
BASP162
BHOH550
BHOH551
BHOH559
BHOH564
BHOH565

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGAFSEVIlAedkrtqklvaik......CIAK
ChainResidueDetails
ALEU26-LYS53

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLY
ChainResidueDetails
AILE137-TYR149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
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 Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMKK1 and CaMKK2","evidences":[{"source":"PubMed","id":"7641687","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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