2IVT

Crystal structure of phosphorylated RET tyrosine kinase domain

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	14
Details	BINDING SITE FOR RESIDUE AMP A3015

Chain	Residue
A	LEU730
A	ARG878
A	ASN879
A	LEU881
A	ASP892
A	HOH2062
A	GLY731
A	GLU732
A	GLY733
A	VAL738
A	ALA756
A	LYS758
A	GLU805
A	ALA807

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A3013

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

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A3014

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

---

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	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP874

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924, ECO:0007744|PDB:4CKI

Chain	Residue	Details
A	LEU730

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924

Chain	Residue	Details
A	LYS758

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:20117004, ECO:0007744|PDB:2X2M

Chain	Residue	Details
A	GLU805

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Cleavage; by caspase-3 => ECO:0000269|PubMed:21357690

Chain	Residue	Details
A	ASP707

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Breakpoint for translocation to form PCM1-RET; RET-CCDC6; RET-GOLGA5; RET-TRIM24 and RET-TRIM33 oncogenes => ECO:0000269|PubMed:10439047, ECO:0000269|PubMed:10980597, ECO:0000269|PubMed:2406025, ECO:0000269|PubMed:2734021

Chain	Residue	Details
A	LEU712

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813

Chain	Residue	Details
A	TYR806
A	TYR809

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24560924

Chain	Residue	Details
A	TYR826

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:24560924

Chain	Residue	Details
A	TYR900

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:20117004, ECO:0000269|PubMed:24560924, ECO:0000269|PubMed:28846099

Chain	Residue	Details
A	PTR905

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:24560924

Chain	Residue	Details
A	TYR981

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP874
A	ARG878

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP874
A	ALA876

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASN879
A	ASP874
A	ALA876

---