Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5DST

Crystal structure of human PRMT8 in complex with SAH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016274	molecular_function	protein-arginine N-methyltransferase activity
A	0018216	biological_process	peptidyl-arginine methylation
B	0016274	molecular_function	protein-arginine N-methyltransferase activity
B	0018216	biological_process	peptidyl-arginine methylation
C	0016274	molecular_function	protein-arginine N-methyltransferase activity
C	0018216	biological_process	peptidyl-arginine methylation
D	0016274	molecular_function	protein-arginine N-methyltransferase activity
D	0018216	biological_process	peptidyl-arginine methylation
E	0016274	molecular_function	protein-arginine N-methyltransferase activity
E	0018216	biological_process	peptidyl-arginine methylation
F	0016274	molecular_function	protein-arginine N-methyltransferase activity
F	0018216	biological_process	peptidyl-arginine methylation
G	0016274	molecular_function	protein-arginine N-methyltransferase activity
G	0018216	biological_process	peptidyl-arginine methylation
H	0016274	molecular_function	protein-arginine N-methyltransferase activity
H	0018216	biological_process	peptidyl-arginine methylation
I	0016274	molecular_function	protein-arginine N-methyltransferase activity
I	0018216	biological_process	peptidyl-arginine methylation
J	0016274	molecular_function	protein-arginine N-methyltransferase activity
J	0018216	biological_process	peptidyl-arginine methylation
K	0016274	molecular_function	protein-arginine N-methyltransferase activity
K	0018216	biological_process	peptidyl-arginine methylation
L	0016274	molecular_function	protein-arginine N-methyltransferase activity
L	0018216	biological_process	peptidyl-arginine methylation
M	0016274	molecular_function	protein-arginine N-methyltransferase activity
M	0018216	biological_process	peptidyl-arginine methylation
N	0016274	molecular_function	protein-arginine N-methyltransferase activity
N	0018216	biological_process	peptidyl-arginine methylation
O	0016274	molecular_function	protein-arginine N-methyltransferase activity
O	0018216	biological_process	peptidyl-arginine methylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue SAH A 401

Chain	Residue
A	TYR80
A	GLU141
A	CYS142
A	GLY167
A	LYS168
A	VAL169
A	GLU170
A	GLU185
A	MET196
A	THR199
A	HIS86
A	MET89
A	ARG95
A	GLY119
A	SER120
A	THR122
A	ILE124
A	LEU125

site_id	AC2
Number of Residues	15
Details	binding site for residue SAH B 401

Chain	Residue
B	TYR80
B	HIS86
B	MET89
B	ARG95
B	GLY119
B	SER120
B	ILE124
B	LEU125
B	GLU141
B	CYS142
B	VAL169
B	GLU170
B	GLU185
B	MET196
B	THR199

site_id	AC3
Number of Residues	17
Details	binding site for residue SAH C 401

Chain	Residue
C	TYR80
C	HIS86
C	MET89
C	ARG95
C	GLY119
C	SER120
C	THR122
C	ILE124
C	LEU125
C	GLU141
C	CYS142
C	GLY167
C	LYS168
C	VAL169
C	GLU170
C	MET196
C	THR199

site_id	AC4
Number of Residues	18
Details	binding site for residue SAH D 401

Chain	Residue
D	TYR80
D	HIS86
D	MET89
D	ARG95
D	GLY119
D	SER120
D	THR122
D	ILE124
D	LEU125
D	GLU141
D	CYS142
D	SER143
D	GLY167
D	LYS168
D	VAL169
D	GLU170
D	MET196
D	THR199

site_id	AC5
Number of Residues	15
Details	binding site for residue SAH E 401

Chain	Residue
E	TYR80
E	HIS86
E	MET89
E	ARG95
E	GLY119
E	SER120
E	THR122
E	ILE124
E	LEU125
E	GLU141
E	CYS142
E	VAL169
E	GLU170
E	MET196
E	THR199

site_id	AC6
Number of Residues	17
Details	binding site for residue SAH F 401

Chain	Residue
F	THR199
F	TYR80
F	HIS86
F	MET89
F	ARG95
F	GLY119
F	SER120
F	THR122
F	ILE124
F	LEU125
F	GLU141
F	CYS142
F	GLY167
F	VAL169
F	GLU170
F	GLU185
F	MET196

site_id	AC7
Number of Residues	17
Details	binding site for residue SAH G 401

Chain	Residue
G	TYR80
G	HIS86
G	ARG95
G	GLY119
G	SER120
G	THR122
G	ILE124
G	LEU125
G	GLU141
G	CYS142
G	GLY167
G	LYS168
G	VAL169
G	GLU170
G	GLU185
G	MET196
G	THR199

site_id	AC8
Number of Residues	16
Details	binding site for residue SAH H 401

Chain	Residue
H	TYR80
H	MET89
H	ARG95
H	GLY119
H	SER120
H	THR122
H	ILE124
H	LEU125
H	GLU141
H	CYS142
H	GLY167
H	LYS168
H	VAL169
H	GLU170
H	MET196
H	THR199

site_id	AC9
Number of Residues	17
Details	binding site for residue SAH I 401

Chain	Residue
I	TYR80
I	MET89
I	ARG95
I	GLY119
I	SER120
I	GLY121
I	THR122
I	ILE124
I	LEU125
I	GLU141
I	CYS142
I	GLY167
I	LYS168
I	VAL169
I	GLU170
I	MET196
I	THR199

site_id	AD1
Number of Residues	16
Details	binding site for residue SAH J 401

Chain	Residue
J	TYR80
J	MET89
J	ARG95
J	GLY119
J	SER120
J	THR122
J	ILE124
J	LEU125
J	GLU141
J	CYS142
J	GLY167
J	LYS168
J	VAL169
J	GLU170
J	MET196
J	THR199

site_id	AD2
Number of Residues	16
Details	binding site for residue SAH K 401

Chain	Residue
K	TYR80
K	HIS86
K	ARG95
K	GLY119
K	SER120
K	THR122
K	ILE124
K	LEU125
K	GLU141
K	CYS142
K	GLY167
K	LYS168
K	VAL169
K	GLU170
K	MET196
K	THR199

site_id	AD3
Number of Residues	17
Details	binding site for residue SAH L 401

Chain	Residue
L	TYR80
L	HIS86
L	MET89
L	ARG95
L	GLY119
L	SER120
L	THR122
L	ILE124
L	LEU125
L	GLU141
L	CYS142
L	GLY167
L	VAL169
L	GLU170
L	GLU185
L	MET196
L	THR199

site_id	AD4
Number of Residues	17
Details	binding site for residue SAH M 401

Chain	Residue
M	TYR80
M	HIS86
M	MET89
M	ARG95
M	GLY119
M	SER120
M	THR122
M	ILE124
M	LEU125
M	GLU141
M	CYS142
M	SER143
M	VAL169
M	GLU170
M	GLU185
M	MET196
M	THR199

site_id	AD5
Number of Residues	14
Details	binding site for residue SAH N 401

Chain	Residue
N	TYR80
N	HIS86
N	ARG95
N	GLY119
N	SER120
N	THR122
N	LEU125
N	GLU141
N	CYS142
N	GLY167
N	VAL169
N	GLU170
N	MET196
N	THR199

site_id	AD6
Number of Residues	19
Details	binding site for residue SAH O 401

Chain	Residue
O	TYR80
O	HIS86
O	MET89
O	ARG95
O	GLY119
O	SER120
O	GLY121
O	THR122
O	ILE124
O	LEU125
O	GLU141
O	CYS142
O	GLY167
O	LYS168
O	VAL169
O	GLU170
O	GLU185
O	MET196
O	THR199

Functional Information from PROSITE/UniProt

site_id	PS00329
Number of Residues	14
Details	HSP70_2 Heat shock hsp70 proteins family signature 2. VLDVGSGTgilSMF

Chain	Residue	Details
A	VAL115-PHE128

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	ACT_SITE: ACT_SITE => ECO:0000250\|UniProtKB:Q63009

Chain	Residue	Details
A	GLU185
E	GLU194
F	GLU185
F	GLU194
G	GLU185
G	GLU194
H	GLU185
H	GLU194
I	GLU185
I	GLU194
J	GLU185
A	GLU194
J	GLU194
K	GLU185
K	GLU194
L	GLU185
L	GLU194
M	GLU185
M	GLU194
N	GLU185
N	GLU194
O	GLU185
B	GLU185
O	GLU194
B	GLU194
C	GLU185
C	GLU194
D	GLU185
D	GLU194
E	GLU185

site_id	SWS_FT_FI2
Number of Residues	15
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q63009

Chain	Residue	Details
A	HIS86
J	HIS86
K	HIS86
L	HIS86
M	HIS86
N	HIS86
O	HIS86
B	HIS86
C	HIS86
D	HIS86
E	HIS86
F	HIS86
G	HIS86
H	HIS86
I	HIS86

site_id	SWS_FT_FI3
Number of Residues	30
Details	BINDING: BINDING => ECO:0000305\|PubMed:26529540, ECO:0000305\|PubMed:26876602, ECO:0007744\|PDB:4X41, ECO:0007744\|PDB:5DST

Chain	Residue	Details
A	ARG95
E	GLU141
F	ARG95
F	GLU141
G	ARG95
G	GLU141
H	ARG95
H	GLU141
I	ARG95
I	GLU141
J	ARG95
A	GLU141
J	GLU141
K	ARG95
K	GLU141
L	ARG95
L	GLU141
M	ARG95
M	GLU141
N	ARG95
N	GLU141
O	ARG95
B	ARG95
O	GLU141
B	GLU141
C	ARG95
C	GLU141
D	ARG95
D	GLU141
E	ARG95

site_id	SWS_FT_FI4
Number of Residues	30
Details	BINDING: BINDING => ECO:0000305\|PubMed:26876602, ECO:0007744\|PDB:5DST

Chain	Residue	Details
A	GLY119
E	GLU170
F	GLY119
F	GLU170
G	GLY119
G	GLU170
H	GLY119
H	GLU170
I	GLY119
I	GLU170
J	GLY119
A	GLU170
J	GLU170
K	GLY119
K	GLU170
L	GLY119
L	GLU170
M	GLY119
M	GLU170
N	GLY119
N	GLU170
O	GLY119
B	GLY119
O	GLU170
B	GLU170
C	GLY119
C	GLU170
D	GLY119
D	GLU170
E	GLY119

site_id	SWS_FT_FI5
Number of Residues	15
Details	MOD_RES: Asymmetric dimethylarginine; by autocatalysis => ECO:0000269\|PubMed:17925405

Chain	Residue	Details
A	ARG73
J	ARG73
K	ARG73
L	ARG73
M	ARG73
N	ARG73
O	ARG73
B	ARG73
C	ARG73
D	ARG73
E	ARG73
F	ARG73
G	ARG73
H	ARG73
I	ARG73

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