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4CNH

Structure of the Human Anaplastic Lymphoma Kinase in Complex with the inhibitor 3-((1R)-1-(5-fluoro-2-methoxyphenyl)ethoxy)-5-(1-methyl-1H- 1,2,3-triazol-5-yl)pyridin-2-amine

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
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3U9 B 2401
ChainResidue
BHIS1124
BLEU1256
BGLY1269
BASP1270
BVAL1130
BALA1148
BLEU1196
BGLU1197
BMET1199
BGLY1202
BARG1253
BASN1254

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 3U9 A 2402
ChainResidue
ALEU1122
AALA1148
AGLU1197
AMET1199
AARG1253
AASN1254
ALEU1256
AGLY1269
AASP1270

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3U9 B 2402
ChainResidue
AHOH2163
AHOH2164
BTYR1096
BASP1163
BMET1166
BGLU1167
BPHE1271
BARG1275
BTYR1278
BARG1279

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP1249
BASP1249

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AHIS1124
AGLU1197
BHIS1124
BGLU1197

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS1150
BLYS1150

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20632993
ChainResidueDetails
AASP1270
BASP1270

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16878150, ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR1096
BTYR1096

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR1131
BTYR1131

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15938644
ChainResidueDetails
ATYR1278
BTYR1278

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PDB entries from 2024-04-24

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