Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4CKJ

Crystal structure of RET tyrosine kinase domain bound to adenosine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADN A 2014

Chain	Residue
A	LEU730
A	HOH3069
A	HOH3073
A	GLY731
A	ALA756
A	GLU805
A	ALA807
A	SER811
A	LEU881
A	FMT2016
A	HOH3053

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 2015

Chain	Residue
A	LYS728
A	LYS740
A	TYR806
A	FMT2016

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 2016

Chain	Residue
A	LEU730
A	ALA807
A	LYS808
A	GLY810
A	ADN2014
A	FMT2015

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 2017

Chain	Residue
A	LYS722
A	LYS722
A	ASN723
A	ARG908
A	FMT2023

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 2018

Chain	Residue
A	LYS737
A	LYS761
A	GLU762

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT A 2019

Chain	Residue
A	GLY700
A	PRO701
A	LEU702
A	SER703
A	GLN910
A	LEU923
A	PHE924
A	HIS926

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 2020

Chain	Residue
A	ARG770
A	LYS907
A	SER909
A	GLN910
A	ARG912
A	HOH3040

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 2021

Chain	Residue
A	THR946
A	LEU947
A	GLY948

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 2022

Chain	Residue
A	ARG873
A	LEU895
A	LYS907
A	GLY911
A	ARG912

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 2023

Chain	Residue
A	LYS722
A	ARG908
A	ARG908
A	FMT2017

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT A 2024

Chain	Residue
A	PRO766
A	SER909
A	GLN910
A	GLY911
A	SER922
A	HIS926
A	TYR928
A	HOH3080

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 2025

Chain	Residue
A	SER703
A	PHE961
A	LYS965
A	HOH3106

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 2026

Chain	Residue
A	ASP903
A	THR929
A	THR930

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 2027

Chain	Residue
A	ARG770
A	LEU773
A	SER774

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 2028

Chain	Residue
A	LYS808
A	TYR809
A	GLU884
A	GLY885

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT A 2029

Chain	Residue
A	HIS786
A	GLN860

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 2030

Chain	Residue
A	LEU779
A	VAL782
A	ILE788
A	LYS789
A	LEU790
A	HOH3044
A	HOH3046

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGEFGKVVkAtafhlkgragytt.....VAVK

Chain	Residue	Details
A	LEU730-LYS758

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNILV

Chain	Residue	Details
A	LEU870-VAL882

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4CKI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20117004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X2M","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Cleavage; by caspase-3","evidences":[{"source":"PubMed","id":"21357690","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Breakpoint for translocation to form PCM1-RET; RET-CCDC6; RET-GOLGA5; RET-TRIM24 and RET-TRIM33 oncogenes","evidences":[{"source":"PubMed","id":"10439047","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10980597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2406025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2734021","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)