Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8BB1

T3 SAM lyase in complex with S-adenosylmethionine synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004478	molecular_function	methionine adenosyltransferase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006556	biological_process	S-adenosylmethionine biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0016740	molecular_function	transferase activity
A	0030955	molecular_function	potassium ion binding
A	0033353	biological_process	S-adenosylmethionine cycle
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004478	molecular_function	methionine adenosyltransferase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006556	biological_process	S-adenosylmethionine biosynthetic process
B	0006730	biological_process	one-carbon metabolic process
B	0016740	molecular_function	transferase activity
B	0030955	molecular_function	potassium ion binding
B	0033353	biological_process	S-adenosylmethionine cycle
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004478	molecular_function	methionine adenosyltransferase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006556	biological_process	S-adenosylmethionine biosynthetic process
C	0006730	biological_process	one-carbon metabolic process
C	0016740	molecular_function	transferase activity
C	0030955	molecular_function	potassium ion binding
C	0033353	biological_process	S-adenosylmethionine cycle
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0004478	molecular_function	methionine adenosyltransferase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006556	biological_process	S-adenosylmethionine biosynthetic process
D	0006730	biological_process	one-carbon metabolic process
D	0016740	molecular_function	transferase activity
D	0030955	molecular_function	potassium ion binding
D	0033353	biological_process	S-adenosylmethionine cycle
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
E	0016740	molecular_function	transferase activity
E	0016829	molecular_function	lyase activity
E	0047625	molecular_function	S-adenosyl-L-methionine lyase activity
F	0016740	molecular_function	transferase activity
F	0016829	molecular_function	lyase activity
F	0047625	molecular_function	S-adenosyl-L-methionine lyase activity
G	0016740	molecular_function	transferase activity
G	0016829	molecular_function	lyase activity
G	0047625	molecular_function	S-adenosyl-L-methionine lyase activity
H	0016740	molecular_function	transferase activity
H	0016829	molecular_function	lyase activity
H	0047625	molecular_function	S-adenosyl-L-methionine lyase activity

Functional Information from PROSITE/UniProt

site_id	PS00376
Number of Residues	11
Details	ADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY

Chain	Residue	Details
A	GLY115-TYR125

site_id	PS00377
Number of Residues	9
Details	ADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD

Chain	Residue	Details
A	GLY258-ASP266

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_00086, ECO:0000269\|PubMed:14967023, ECO:0007744\|PDB:1P7L, ECO:0007744\|PDB:1RG9

Chain	Residue	Details
A	HIS14
B	GLN98
B	ASP163
B	ARG229
B	ARG244
B	LYS269
C	HIS14
C	GLU55
C	GLN98
C	ASP163
C	ARG229
A	GLU55
C	ARG244
C	LYS269
D	HIS14
D	GLU55
D	GLN98
D	ASP163
D	ARG229
D	ARG244
D	LYS269
A	GLN98
A	ASP163
A	ARG229
A	ARG244
A	LYS269
B	HIS14
B	GLU55

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00086, ECO:0000269\|PubMed:14967023, ECO:0007744\|PDB:1P7L, ECO:0007744\|PDB:1RG9

Chain	Residue	Details
A	ASP16
D	ASP16
D	ALA261
D	LYS265
A	ALA261
A	LYS265
B	ASP16
B	ALA261
B	LYS265
C	ASP16
C	ALA261
C	LYS265

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00086, ECO:0000269\|PubMed:14967023, ECO:0000305\|PubMed:7629147, ECO:0007744\|PDB:1MXC, ECO:0007744\|PDB:1P7L, ECO:0007744\|PDB:1RG9

Chain	Residue	Details
A	GLU42
B	GLU42
C	GLU42
D	GLU42

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00086, ECO:0000269\|PubMed:14967023, ECO:0007744\|PDB:1P7L

Chain	Residue	Details
A	ASP238
B	ASP238
C	ASP238
D	ASP238

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	LYS2
B	LYS2
C	LYS2
D	LYS2

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)