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8S9P

1:1:1 agrin/LRP4/MuSK complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0043113biological_processreceptor clustering
A0043236molecular_functionlaminin binding
B0005509molecular_functioncalcium ion binding
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CtNsegaFqCwC
ChainResidueDetails
BCYS409-CYS420

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CsCrpGvgGLrC
ChainResidueDetails
ACYS812-CYS823
ACYS866-CYS877
ACYS1355-CYS1366
ACYS1574-CYS1585
ACYS1613-CYS1624
ACYS1845-CYS1856

site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAFGRVFqArapgllpyepftm.....VAVK
ChainResidueDetails
CILE581-LYS609

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLATRNCLV
ChainResidueDetails
CPHE721-VAL733

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREL
ChainResidueDetails
CMET1-LEU4

site_idPS01148
Number of Residues25
DetailsUPF0033 Uncharacterized protein family UPF0033 signature. LDaeGsnCPaTkVfqgvlelegveG
ChainResidueDetails
ALEU1121-GLY1145

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. ClCpgGFsgph....C
ChainResidueDetails
ACYS1845-CYS1856
BCYS378-CYS393
BCYS418-CYS433
BCYS722-CYS736

site_idPS01187
Number of Residues24
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvNECaeegy.........Csqg....CtNsegaFqC
ChainResidueDetails
BASP395-CYS418

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpaqwq.CDgdnDCgdhsDEDg....C
ChainResidueDetails
BCYS44-CYS66
BCYS83-CYS105
BCYS122-CYS143
BCYS160-CYS182
BCYS203-CYS225
BCYS243-CYS265
BCYS282-CYS304
BCYS324-CYS349

site_idPS01248
Number of Residues36
DetailsEGF_LAM_1 Laminin-type EGF-like (LE) domain signature. Cs.CrpgvgGlrCdrCepgfWnfrgivtdgrsgctpC
ChainResidueDetails
ACYS812-CYS847

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues471
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
CLEU24-THR495
ALEU1957
AGLN2007
AASP2009

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
CVAL496-TYR516

site_idSWS_FT_FI3
Number of Residues352
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
CCYS517-VAL869

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
CASP725
BASN498
BASN719
BASN901
BASN1077
BASN1415
BASN1467

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
CILE581
CLYS609

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q61006
ChainResidueDetails
CTYR554

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:Q61006
ChainResidueDetails
CSER681
CSER698

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q62838
ChainResidueDetails
CTYR755

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN222
ASER676

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250
ChainResidueDetails
CASN338

site_idSWS_FT_FI11
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN250
AASN777
AASN932

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) serine => ECO:0000250|UniProtKB:P25304
ChainResidueDetails
ASER1835

224931

PDB entries from 2024-09-11

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