4D2T

Structure of MELK in complex with inhibitors

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 3I7 D 1334

Chain	Residue
D	ILE17
D	HOH2021
D	ALA38
D	GLU87
D	TYR88
D	CYS89
D	PRO90
D	GLY92
D	LEU139
D	ILE149

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 3I7 A 1334

Chain	Residue
A	ALA23
A	VAL25
A	LEU27
A	ALA38
A	LYS40
A	GLU57
A	CYS70
A	GLU87
A	TYR88
A	CYS89
A	PRO90
A	ILE149
A	ASP150

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3I7 B 1334

Chain	Residue
B	ILE17
B	LEU27
B	ALA38
B	GLU87
B	CYS89
B	PRO90
B	ILE149
B	HOH2028

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3I7 C 1334

Chain	Residue
B	GLY18
B	THR19
C	ILE17
C	ALA38
C	LYS40
C	GLU87
C	TYR88
C	CYS89
C	PRO90
C	GLU93
C	ILE149

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE17-LYS40

---

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

Chain	Residue	Details
A	TYR128-PHE140

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP132
B	ASP132
C	ASP132
D	ASP132

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE17
A	LYS40
B	ILE17
B	LYS40
C	ILE17
C	LYS40
D	ILE17
D	LYS40

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	THR56
B	THR56
C	THR56
D	THR56

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	TYR163
B	TYR163
C	TYR163
D	TYR163

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:16628004

Chain	Residue	Details
A	ALA167
B	ALA167
C	ALA167
D	ALA167

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	ALA171
D	ALA171
D	SER253
D	SER336
A	SER253
A	SER336
B	ALA171
B	SER253
B	SER336
C	ALA171
C	SER253
C	SER336

---