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5KMM

TrkA JM-kinase with 1-(2-methyl-4-phenyl-pyrimidin-5-yl)-3-(1-naphthyl)urea

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 6UJ A 901
ChainResidue
ASER484
ALEU486
APHE521
AGLU560
ALEU564
APHE646
AHIS648
AASP668
AGLY670

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVFlAechnllpeqdkml.....VAVK
ChainResidueDetails
ALEU516-LYS544

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLATRNCLV
ChainResidueDetails
APHE646-VAL658

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYstdYYR
ChainResidueDetails
AASP674-ARG682

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLY522-ASP537

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AARG748

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AGLY614
AALA642

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Breakpoint for translocation to form TRK and TRK-T3
ChainResidueDetails
ATYR496

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Breakpoint for translocation to form TRK-T1
ChainResidueDetails
APRO584

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Interaction with SHC1
ChainResidueDetails
AHIS594

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:8155326
ChainResidueDetails
AHIS594

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8155326
ChainResidueDetails
AILE774

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:8155326
ChainResidueDetails
AHIS778
AALA779

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASP499

221716

PDB entries from 2024-06-26

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