5F20

Structure of TYK2 with inhibitor 4: 3-azanyl-5-(2-methylphenyl)-7-(1-methylpyrazol-3-yl)-1~{H}-pyrazolo[4,3-c]pyridin-4-one

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein 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	12
Details	binding site for residue 5U4 A 1200

Chain	Residue
A	ARG901
A	GLY984
A	ARG1027
A	LEU1030
A	LEU903
A	GLU905
A	GLY906
A	ILE960
A	GLU979
A	TYR980
A	VAL981
A	PRO982

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGHFGKVSlYcydptndgtgem......VAVK

Chain	Residue	Details
A	LEU903-LYS930

---

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	ASN1023

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU903
A	LYS930

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER884

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20478313, ECO:0000269|PubMed:8702790

Chain	Residue	Details
A	TYR1054

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8702790

Chain	Residue	Details
A	TYR1055

---