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3KN6

Crystal structure of the C-terminal kinase domain of MSK1

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 PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFSICRkCvhkksnqa..........FAVK
ChainResidueDetails
ALEU432-LYS455

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNLLF
ChainResidueDetails
AVAL540-PHE552

site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VKLHEVFHDQ
ChainResidueDetails
AVAL482-GLN491

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASP544
BASP544

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU432
ALYS455
BLEU432
BLYS455

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by MAPK1, MAPK3 and MAPK14 => ECO:0000269|PubMed:15568999
ChainResidueDetails
ATHR581
BTHR581

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17117922
ChainResidueDetails
ASER647
ASER657
ASER695
BSER647
BSER657
BSER695

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8C050
ChainResidueDetails
ASER691
BSER691

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by MAPK1, MAPK3 and MAPK14 => ECO:0000269|PubMed:17117922
ChainResidueDetails
ATHR700
BTHR700

219140

PDB entries from 2024-05-01

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