Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6QAV

Crystal structure of ULK2 in complexed with MRT68921

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	0010506	biological_process	regulation of autophagy
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	0010506	biological_process	regulation of autophagy
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	0010506	biological_process	regulation of autophagy
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	0010506	biological_process	regulation of autophagy

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue HVH A 301

Chain	Residue
A	VAL15
A	GLY91
A	ASP95
A	GLN135
A	LEU138
A	ALA157
A	ASP158
A	HOH447
A	HOH473
A	HIS17
A	GLY18
A	VAL23
A	ALA37
A	MET85
A	GLU86
A	TYR87
A	CYS88

site_id	AC2
Number of Residues	6
Details	binding site for residue EDO A 302

Chain	Residue
A	LYS39
A	ILE41
A	LEU53
A	GLU56
A	GLY160
A	HOH432

site_id	AC3
Number of Residues	2
Details	binding site for residue EDO A 303

Chain	Residue
A	ASP192
A	HOH462

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO A 304

Chain	Residue
A	LYS43
A	ASN79
A	HOH446
B	GLU76

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO A 305

Chain	Residue
A	ASN89
A	GLY90
A	GLY91
A	ASP95

site_id	AC6
Number of Residues	16
Details	binding site for residue HVH B 301

Chain	Residue
B	VAL15
B	HIS17
B	GLY18
B	ALA37
B	LYS39
B	MET85
B	GLU86
B	TYR87
B	CYS88
B	GLY91
B	ASP92
B	ASP95
B	GLN135
B	LEU138
B	ASP158
B	HOH414

site_id	AC7
Number of Residues	6
Details	binding site for residue NA B 302

Chain	Residue
B	LEU60
B	LYS61
B	LEU63
B	HOH444
B	HOH466
B	HOH483

site_id	AC8
Number of Residues	6
Details	binding site for residue EDO B 303

Chain	Residue
B	MET1
B	VAL3
B	GLU8
B	ARG29
D	EDO304
D	HOH408

site_id	AC9
Number of Residues	3
Details	binding site for residue EDO B 304

Chain	Residue
B	LYS61
B	LEU71
B	HOH444

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO B 305

Chain	Residue
B	SER104
B	GLU105
B	LEU208
B	HOH409
B	HOH453

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO B 306

Chain	Residue
B	GLY54
B	LYS55
B	GLU56
B	ILE57
B	GOL307
B	HOH438

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL B 307

Chain	Residue
B	LYS39
B	GLY54
B	GLY160
B	EDO306
B	HOH401
B	HOH438

site_id	AD4
Number of Residues	18
Details	binding site for residue HVH C 301

Chain	Residue
C	VAL15
C	GLY16
C	HIS17
C	GLY18
C	VAL23
C	ALA37
C	MET85
C	GLU86
C	TYR87
C	CYS88
C	GLY91
C	ASP92
C	ASP95
C	GLN135
C	LEU138
C	ASP158
C	HOH449
C	HOH486

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO C 302

Chain	Residue
C	LYS39
C	ILE41
C	GLU56
C	GLY160
C	HOH459

site_id	AD6
Number of Residues	5
Details	binding site for residue EDO C 303

Chain	Residue
C	SER104
C	GLU105
C	HOH410
C	HOH441
C	HOH447

site_id	AD7
Number of Residues	5
Details	binding site for residue EDO C 304

Chain	Residue
A	TYR243
C	ILE236
C	PRO237
C	ARG238
C	THR240

site_id	AD8
Number of Residues	5
Details	binding site for residue GOL C 305

Chain	Residue
A	GLN75
C	GLU8
C	HOH406
C	HOH434
C	HOH443

site_id	AD9
Number of Residues	14
Details	binding site for residue HVH D 301

Chain	Residue
D	VAL15
D	HIS17
D	GLY18
D	ALA37
D	MET85
D	GLU86
D	TYR87
D	CYS88
D	GLY91
D	ASP95
D	GLN135
D	LEU138
D	ASP158
D	HOH422

site_id	AE1
Number of Residues	2
Details	binding site for residue EDO D 302

Chain	Residue
D	ARG144
D	SER147

site_id	AE2
Number of Residues	6
Details	binding site for residue EDO D 303

Chain	Residue
D	ALA19
D	LEU52
D	LEU53
D	GLY54
D	GLY160
D	HOH435

site_id	AE3
Number of Residues	5
Details	binding site for residue EDO D 304

Chain	Residue
B	EDO303
D	VAL74
D	GLU76
D	HOH408
D	HOH453

site_id	AE4
Number of Residues	2
Details	binding site for residue EDO D 305

Chain	Residue
C	SER47
D	GLU76

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGHGAFAVVFrGrhrqktdwe.........VAIK

Chain	Residue	Details
A	VAL15-LYS39

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

Chain	Residue	Details
A	ILE127-LEU139

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	ASP131
B	ASP131
C	ASP131
D	ASP131

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

Chain	Residue	Details
A	VAL15
B	VAL15
C	VAL15
D	VAL15

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS39
B	LYS39
C	LYS39
D	LYS39

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