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7JYT

hALK in complex with 3-(3-methyl-1H-pyrazol-5-yl)pyridine

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 Residues7
Detailsbinding site for residue GOL A 1501
ChainResidue
AILE1171
APHE1174
AASN1175
AARG1181
ACYS1182
ALEU1224
AHOH1621

site_idAC2
Number of Residues5
Detailsbinding site for residue VRM A 1502
ChainResidue
AGLU1197
AMET1199
AGLY1202
AALA1148
ALEU1196

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
AHIS1124
AGLU1197

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:0000250|UniProtKB:P97793
ChainResidueDetails
ATYR1092

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16878150, ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR1096

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR1131

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15938644
ChainResidueDetails
ATYR1278

226707

PDB entries from 2024-10-30

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