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1LUF

Crystal Structure of the MuSK Tyrosine Kinase: Insights into Receptor Autoregulation

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAFGRVFqArapgllpyepftm.....VAVK
ChainResidueDetails
AILE580-LYS608

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLATRNCLV
ChainResidueDetails
APHE720-VAL732

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:PRU10028
ChainResidueDetails
AASP724

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE580
ALYS608

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q61006
ChainResidueDetails
ATYR553

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:Q61006
ChainResidueDetails
ASER680
ASER697

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20603078
ChainResidueDetails
ATYR754

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP724
AARG728

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA726
AASP724

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN729
AALA726
AASP724

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PDB entries from 2024-09-18

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