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4BFM

The crystal structure of mouse PK38

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ANP A 1000
ChainResidue
AILE17
ALYS40
ACYS70
AGLU87
ACYS89
AGLU93
ALEU139
AASP150
AHOH3082
AGLY18
ATHR19
AGLY20
AGLY21
APHE22
AALA23
AVAL25
AALA38

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2001
ChainResidue
AGLU15
ATHR16
ALYS26
ATYR122
AHOH3076

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AHIS68
ALYS145
AHOH3044

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
ASER105
AGLU106
AGLU107
AHOH3030
AHOH3061

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2004
ChainResidue
ASER296
ASER297
ATHR300
AHOH3078

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2006
ChainResidue
AALA121
AMET254
ATRP273
ASO42007

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2007
ChainResidue
AHIS124
ASER188
AMET254
ASO42006

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGTGGFAKVKlAchvltgem..........VAIK
ChainResidueDetails
AILE17-LYS40

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKpeNLLF
ChainResidueDetails
ATYR128-PHE140

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
AASP132

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS40
AILE17

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:Q14680
ChainResidueDetails
AGLU167
ATHR56

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q14680
ChainResidueDetails
ATYR163

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q14680
ChainResidueDetails
ASER253
ASER171

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PDB entries from 2024-05-15

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