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3AOX

X-ray crystal structure of human anaplastic lymphoma kinase in complex with CH5424802

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 Residues11
DetailsBINDING SITE FOR RESIDUE EMH A 901
ChainResidue
AEDO802
ALEU1256
AGLY1269
AARG1120
ALEU1122
AALA1148
ALEU1196
AGLU1197
ALEU1198
AMET1199
AALA1200

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 801
ChainResidue
AHOH185
AASN1353
ATHR1395
AALA1396

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 802
ChainResidue
AHOH153
AHOH239
AEMH901
AARG1253
AGLY1269

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 803
ChainResidue
AHOH215
AVAL1293
AGLN1336

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 804
ChainResidue
AGLY1123
AVAL1130

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20632993","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P97793","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"16878150","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15938644","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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