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4F99

Human CDC7 kinase in complex with DBF4 and nucleotide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0003676molecular_functionnucleic acid binding
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ADP A 601
ChainResidue
AILE64
ALEU137
AHIS139
ASER181
AASN182
AASP196
AMG602
AHOH701
AHOH702
AGLY67
ASER70
AVAL72
AALA88
ALYS90
AMET118
APRO135
ATYR136

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 602
ChainResidue
AASN182
AASP196
AADP601
AHOH701
AHOH702

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BCYS296
BCYS299
BHIS309
BHIS315

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTFSSVYlAtaqlqvgpeek.......IALK
ChainResidueDetails
AILE64-LYS90

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDVKpsNFLY
ChainResidueDetails
AILE173-TYR185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsZN_FING: DBF4-type => ECO:0000255|PROSITE-ProRule:PRU00600
ChainResidueDetails
BGLU289-ASP337

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00600
ChainResidueDetails
BCYS296
BCYS299
BHIS309
BHIS315

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR273
BTHR345

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER312

220472

PDB entries from 2024-05-29

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