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3DFC

Crystal structure of a glycine-rich loop mutant of the death associated protein kinase catalytic domain with AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP B 296
ChainResidue
BLEU19
BGLU94
BGLU100
BASP139
BMET146
BILE160
BASP161
BHOH302
BHOH341
BHOH366
BHOH392
BGLY20
BSER21
BGLY22
BLYS23
BPHE24
BALA25
BALA40
BLYS42

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGKFAVVKkCrekstglqyaak......FIKK
ChainResidueDetails
BLEU19-LYS46

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML
ChainResidueDetails
BILE135-LEU147

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
BASP139

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
BLEU19
BLYS42
BGLU94
BGLU100
BASP161

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BGLU143
BASP139

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP139
BLYS141

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR180
BASP139
BLYS141

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP139
BLYS141
BASN144

222926

PDB entries from 2024-07-24

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