Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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	753
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	141
Details	Domain: {"description":"SARAH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00310","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	66
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29063833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6AO5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"20086174","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23972470","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23972470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29063833","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine; by PLK1","evidences":[{"source":"PubMed","id":"21723128","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)