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5FTO

Crystal structure of the ALK kinase domain in complex with Entrectinib

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 Residues17
DetailsBINDING SITE FOR RESIDUE YMX A 2402
ChainResidue
ALEU1122
AGLY1201
AGLY1202
AASP1203
AARG1253
AASN1254
ALEU1256
AGLY1269
AASP1270
AGLY1123
APHE1127
AVAL1130
AALA1148
ALEU1196
AGLU1197
AMET1199
AALA1200

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGHGAFGEVYeGqvsgmpndpsplq.....VAVK
ChainResidueDetails
ALEU1122-LYS1150

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDIAARNCLL
ChainResidueDetails
APHE1245-LEU1257

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYrasYYR
ChainResidueDetails
AASP1276-ARG1284

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
AASP1249

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLU1197
AHIS1124

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS1150

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20632993
ChainResidueDetails
AASP1270

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16878150, ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR1096

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR1131

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15938644
ChainResidueDetails
ATYR1278

218500

PDB entries from 2024-04-17

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