3EQB

X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP

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	16
Details	BINDING SITE FOR RESIDUE ATP A9001

Chain	Residue
A	LUG1
A	GLN153
A	LYS192
A	SER194
A	ASN195
A	LEU197
A	ASP208
A	MG9002
A	LEU74
A	GLY77
A	ALA95
A	LYS97
A	MET143
A	GLU144
A	MET146
A	SER150

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A9002

Chain	Residue
A	LUG1
A	LYS97
A	ASN195
A	ASP208
A	ATP9001

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE LUG A 1

Chain	Residue
A	GLY77
A	ASN78
A	LYS97
A	LEU115
A	LEU118
A	VAL127
A	ILE141
A	ASP208
A	PHE209
A	VAL211
A	SER212
A	LEU215
A	ATP9001
A	MG9002

---

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	LEU74-LYS97

---

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

Chain	Residue	Details
A	ILE186-VAL198

---

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	ASP190

---

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	LEU74
A	MET143
A	SER150
A	LYS192
A	ASP208

---

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

Chain	Residue	Details
A	LYS97

---

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

Chain	Residue	Details
A	GLU144
A	SER194

---

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	SER218

---

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	SER222

---

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

Chain	Residue	Details
A	THR286

---

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

Chain	Residue	Details
A	THR292

---

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

Chain	Residue	Details
A	SER298

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	SER194
A	ASP190

---

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

Chain	Residue	Details
A	LYS192
A	ASP190

---

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

Chain	Residue	Details
A	LYS192
A	THR226
A	ASP190

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS192
A	ASN195
A	ASP190

---