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2X2K

Crystal Structure of phosphorylated RET tyrosine kinase domain with inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 2014
ChainResidue
AARG721
AASP797
AGLY798
APRO799
ALEU801

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 2015
ChainResidue
AARG912
AARG873
ALEU895
ALYS907
AGLY911

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 2016
ChainResidue
AGLY700
APRO701
ALEU702
ASER703
AGLN910
ALEU923
APHE924
AHIS926

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE X2K A 2017
ChainResidue
ALEU730
AVAL738
AALA756
ALYS758
AVAL804
AGLU805
ATYR806
AALA807
AGLY810
ALEU881
AASP892

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGEFGKVVkAtafhlkgragytt.....VAVK
ChainResidueDetails
ALEU730-LYS758

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNILV
ChainResidueDetails
ALEU870-VAL882

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 Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4CKI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20117004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X2M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Cleavage; by caspase-3","evidences":[{"source":"PubMed","id":"21357690","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16928683","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16928683","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20117004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28846099","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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