4LGD

Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5

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
A	0007165	biological_process	signal transduction
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
B	0007165	biological_process	signal transduction
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
C	0007165	biological_process	signal transduction
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
D	0007165	biological_process	signal transduction
E	0007165	biological_process	signal transduction
F	0007165	biological_process	signal transduction
G	0007165	biological_process	signal transduction
H	0007165	biological_process	signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP A 501

Chain	Residue
A	LEU33
A	ASP109
A	ASP164
A	MG502
A	GLU35
A	GLY36
A	VAL41
A	ALA54
A	LYS56
A	MET99
A	GLU100
A	CYS102

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	ASP164
A	ANP501

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 503

Chain	Residue
A	ARG145
A	ALA168
A	GLY169
A	GLY197
A	TYR198

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ANP B 501

Chain	Residue
B	GLY36
B	SER37
B	GLY39
B	ALA54
B	LYS56
B	MET99
B	GLU100
B	CYS102
B	ASP109
B	ASP164
B	MG502

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	ASP164
B	ANP501

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 503

Chain	Residue
B	ARG145
B	ALA168
B	GLY169
B	TYR198

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 504

Chain	Residue
B	LEU14
B	SER15
B	SER18
B	HIS46
B	GLU48

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 505

Chain	Residue
B	ASP121
B	ALA124
B	PHE277
B	ASN280
B	ALA281

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 506

Chain	Residue
B	LEU19
B	THR20
B	LYS21
B	GLN22
B	TYR89
B	PHE90
E	ASN379

---

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ANP C 501

Chain	Residue
C	VAL41
C	ALA54
C	LYS56
C	GLU100
C	CYS102
C	ASP109
C	ASP164
C	MG502

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	ASP164
C	ANP501

---

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 503

Chain	Residue
C	ARG145
C	ALA168
C	GLY169
C	GLY197
C	TYR198

---

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE NA C 504

Chain	Residue
C	ASP121

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA C 505

Chain	Residue
C	TYR89
C	PHE90
H	ASN379

---

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP D 501

Chain	Residue
D	GLU35
D	GLY36
D	SER37
D	GLY39
D	VAL41
D	LYS56
D	GLU100
D	CYS102
D	ASP109
D	LEU153
D	ASP164
D	MG502

---

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 502

Chain	Residue
D	ASP164
D	ANP501

---

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 503

Chain	Residue
D	ARG145
D	ALA168
D	GLY169
D	TYR198

---

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 504

Chain	Residue
D	LEU14
D	SER15
D	SER18
D	HIS46
D	GLU48

---

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 505

Chain	Residue
D	LEU19
D	THR20
D	PHE90
G	ASN379

---

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE NA D 506

Chain	Residue
D	ASP121

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU33-LYS56

---

Functional Information from SwissProt/UniProt

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

Chain	Residue	Details
A	ASN146
B	ASN146
C	ASN146
D	ASN146

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU33
B	LEU33
C	LEU33
D	LEU33

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	LYS56
B	LYS56
C	LYS56
D	LYS56

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:29063833, ECO:0007744|PDB:6AO5

Chain	Residue	Details
A	ASN151
A	ASP164
B	ASN151
B	ASP164
C	ASN151
C	ASP164
D	ASN151
D	ASP164

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Cleavage; by caspase-3

Chain	Residue	Details
A	ASP436
B	ASP436
C	ASP436
D	ASP436

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PLK1 => ECO:0000269|PubMed:21723128, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER15
B	SER15
C	SER15
D	SER15

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269|PubMed:20086174

Chain	Residue	Details
A	THR117
B	THR117
C	THR117
D	THR117

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470

Chain	Residue	Details
A	THR174
B	THR174
C	THR174
D	THR174

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23972470, ECO:0000269|PubMed:29063833

Chain	Residue	Details
A	THR180
B	THR180
C	THR180
D	THR180

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	LYS430
B	LYS430
C	LYS430
D	LYS430

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29063833

Chain	Residue	Details
A	MET450
B	MET450
C	MET450
D	MET450

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29063833, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER444
B	SER444
C	SER444
D	SER444

---