3VVH

X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in complex with an inhibitor 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
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 701

Chain	Residue
A	ASN195
A	ASP208
A	ATP702
A	HOH809
A	HOH868

---

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP A 702

Chain	Residue
A	VAL82
A	ALA95
A	LYS97
A	MET143
A	GLU144
A	MET146
A	SER150
A	GLN153
A	LYS192
A	SER194
A	ASN195
A	LEU197
A	ASP208
A	MG701
A	4BM703
A	HOH802
A	HOH809
A	HOH818
A	HOH819
A	HOH868
A	GLY75
A	ALA76
A	GLY77
A	ASN78

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 4BM A 703

Chain	Residue
A	GLY77
A	GLY79
A	GLY80
A	LYS97
A	LEU115
A	VAL127
A	ILE141
A	MET143
A	CYS207
A	ASP208
A	PHE209
A	GLY210
A	VAL211
A	SER212
A	LEU215
A	MET219
A	ATP702
A	HOH809

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 501

Chain	Residue
B	ASN195
B	ASP208
B	ATP502
B	HOH636
B	HOH644

---

site_id	AC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ATP B 502

Chain	Residue
B	LEU74
B	GLY75
B	GLY77
B	ASN78
B	VAL82
B	ALA95
B	LYS97
B	MET143
B	GLU144
B	MET146
B	SER150
B	GLN153
B	LYS192
B	SER194
B	ASN195
B	LEU197
B	ASP208
B	MG501
B	4BM503
B	HOH602
B	HOH621
B	HOH627
B	HOH636
B	HOH639
B	HOH644
B	HOH654

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 4BM B 503

Chain	Residue
B	GLY79
B	GLY80
B	LYS97
B	LEU115
B	VAL127
B	ILE141
B	MET143
B	CYS207
B	ASP208
B	PHE209
B	GLY210
B	VAL211
B	SER212
B	LEU215
B	MET219
B	ATP502
B	HOH644

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 501

Chain	Residue
C	HOH611
C	ASN195
C	ASP208
C	ATP502
C	HOH603

---

site_id	AC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP C 502

Chain	Residue
C	GLY75
C	GLY77
C	ASN78
C	GLY80
C	VAL82
C	ALA95
C	LYS97
C	MET143
C	GLU144
C	MET146
C	SER150
C	GLN153
C	LYS192
C	SER194
C	ASN195
C	LEU197
C	ASP208
C	MG501
C	4BM503
C	HOH601
C	HOH603
C	HOH611
C	HOH615
C	HOH635
C	HOH641

---

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 4BM C 503

Chain	Residue
C	GLY77
C	GLY79
C	GLY80
C	LYS97
C	LEU115
C	VAL127
C	ILE141
C	MET143
C	CYS207
C	ASP208
C	PHE209
C	GLY210
C	VAL211
C	SER212
C	LEU215
C	MET219
C	ATP502
C	HOH603

---

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	3
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP190
B	ASP190
C	ASP190

---

site_id	SWS_FT_FI2
Number of Residues	15
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
B	ASP208
C	LEU74
C	MET143
C	SER150
C	LYS192
C	ASP208
A	MET143
A	SER150
A	LYS192
A	ASP208
B	LEU74
B	MET143
B	SER150
B	LYS192

---

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

Chain	Residue	Details
A	LYS97
B	LYS97
C	LYS97

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF

Chain	Residue	Details
A	GLU144
A	SER194
B	GLU144
B	SER194
C	GLU144
C	SER194

---

site_id	SWS_FT_FI5
Number of Residues	3
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
B	SER218
C	SER218

---

site_id	SWS_FT_FI6
Number of Residues	3
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
B	SER222
C	SER222

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976

Chain	Residue	Details
A	THR286
B	THR286
C	THR286

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986

Chain	Residue	Details
A	THR292
B	THR292
C	THR292

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphoserine; by PAK => ECO:0000269|PubMed:16129686

Chain	Residue	Details
A	SER298
B	SER298
C	SER298

---