3WIG

Human MEK1 kinase in complex with CH5126766 and MgAMP-PNP

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	15
Details	BINDING SITE FOR RESIDUE ANP A 401

Chain	Residue
A	LEU75
A	LYS193
A	SER195
A	ASN196
A	LEU198
A	ASP209
A	MG402
A	ALA77
A	GLY78
A	ALA96
A	LYS98
A	GLU145
A	MET147
A	SER151
A	GLN154

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	ASN196
A	ASP209
A	ANP401

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CHU A 403

Chain	Residue
A	LEU119
A	VAL128
A	GLY129
A	ILE142
A	MET144
A	HIS189
A	ARG190
A	ASP191
A	ASP209
A	PHE210
A	GLY211
A	VAL212
A	SER213
A	LEU216
A	ILE217
A	MET220
A	ASN222

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 A 404

Chain	Residue
A	GLY211
A	VAL212
A	GLY214
A	GLY214
A	GLN215

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 405

Chain	Residue
A	ARG182
A	SER242
A	VAL243

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 406

Chain	Residue
A	THR227

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 407

Chain	Residue
A	PHE371

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 408

Chain	Residue
A	SER331
A	LEU332

---

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 409

Chain	Residue
A	HIS240

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK

Chain	Residue	Details
A	LEU75-LYS98

---

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

Chain	Residue	Details
A	ILE187-VAL199

---

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	ASP191

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613

Chain	Residue	Details
A	LEU75
A	MET144
A	SER151
A	LYS193
A	ASP209

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQH

Chain	Residue	Details
A	LYS98

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF

Chain	Residue	Details
A	GLU145
A	SER195

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746

Chain	Residue	Details
A	SER219

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746

Chain	Residue	Details
A	SER223

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976

Chain	Residue	Details
A	VAL318

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986

Chain	Residue	Details
A	LYS324

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PAK => ECO:0000269|PubMed:16129686

Chain	Residue	Details
A	PHE330

---