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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 Residues39
DetailsRegion: {"description":"UBA-like","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
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_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q14680","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q14680","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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