7NTH

Structure of TAK1 in complex with compound 54

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004672	molecular_function	protein kinase activity
A	0004709	molecular_function	MAP kinase kinase kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007165	biological_process	signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue GOL A 1001

Chain	Residue
A	PRO121
A	GLN299
A	TYR300
A	PRO301
A	HIS495

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site_id	AC2
Number of Residues	7
Details	binding site for residue GOL A 1002

Chain	Residue
A	HOH1158
A	HOH1189
A	HOH1224
A	ARG289
A	TYR290
A	GLN303
A	ASP494

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site_id	AC3
Number of Residues	3
Details	binding site for residue GOL A 1003

Chain	Residue
A	SER132
A	THR169
A	ASP295

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site_id	AC4
Number of Residues	4
Details	binding site for residue DMS A 1004

Chain	Residue
A	PRO258
A	TYR488
A	TRP491
A	HOH1278

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site_id	AC5
Number of Residues	24
Details	binding site for residue URW A 1005

Chain	Residue
A	VAL42
A	GLY43
A	ARG44
A	GLY45
A	LYS63
A	VAL90
A	MET104
A	GLU105
A	TYR106
A	ALA107
A	GLY109
A	GLY110
A	SER111
A	ASN114
A	PRO160
A	LEU162
A	LEU163
A	ASP175
A	HOH1114
A	HOH1131
A	HOH1219
A	HOH1255
A	HOH1267
A	HOH1276

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	22
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGAFGVVCkAkwrakd............VAIK

Chain	Residue	Details
A	VAL42-LYS63

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiHrDLKppNLLL

Chain	Residue	Details
A	LEU152-LEU164

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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:PRU10027

Chain	Residue	Details
A	ASP156

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	VAL42

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	LYS63

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis; alternate => ECO:0000269|PubMed:37832545, ECO:0000305|PubMed:10838074

Chain	Residue	Details
A	THR184

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis; alternate => ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:19675569, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:37832545

Chain	Residue	Details
A	THR187

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:10702308, ECO:0000269|PubMed:10838074

Chain	Residue	Details
A	SER192

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site_id	SWS_FT_FI7
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22406003

Chain	Residue	Details
A	LYS72

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site_id	SWS_FT_FI8
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q62073

Chain	Residue	Details
A	LYS158
A	LYS209

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site_id	SWS_FT_FI9
Number of Residues	1
Details	SITE: Required for interaction with MAP3K7 => ECO:0000269|PubMed:11323434

Chain	Residue	Details
A	PHE484

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