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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6RK7

Inter-dimeric interface controls function and stability of S-methionine adenosyltransferase from U. urealiticum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004478	molecular_function	methionine adenosyltransferase activity
A	0005524	molecular_function	ATP binding
A	0006556	biological_process	S-adenosylmethionine biosynthetic process
B	0004478	molecular_function	methionine adenosyltransferase activity
B	0005524	molecular_function	ATP binding
B	0006556	biological_process	S-adenosylmethionine biosynthetic process
E	0004478	molecular_function	methionine adenosyltransferase activity
E	0005524	molecular_function	ATP binding
E	0006556	biological_process	S-adenosylmethionine biosynthetic process
F	0004478	molecular_function	methionine adenosyltransferase activity
F	0005524	molecular_function	ATP binding
F	0006556	biological_process	S-adenosylmethionine biosynthetic process
G	0004478	molecular_function	methionine adenosyltransferase activity
G	0005524	molecular_function	ATP binding
G	0006556	biological_process	S-adenosylmethionine biosynthetic process
H	0004478	molecular_function	methionine adenosyltransferase activity
H	0005524	molecular_function	ATP binding
H	0006556	biological_process	S-adenosylmethionine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue SAM A 401

Chain	Residue
A	HIS16
A	HOH608
A	HOH634
A	HOH644
B	ALA42
B	GLU57
B	GLN93
B	ASP96
B	ILE97
B	GLY112
B	ASP113
A	PRO17
B	LYS262
B	HOH542
A	ASP158
A	LYS160
A	SER220
A	ARG222
A	PHE223
A	ASP231
A	HOH561

site_id	AC2
Number of Residues	14
Details	binding site for residue SAM A 402

Chain	Residue
A	ILE58
A	THR59
A	THR60
A	HIS61
A	ALA62
A	TYR63
A	VAL64
A	TRP71
A	GLU81
A	ASN82
A	VAL90
A	HOH593
A	HOH640
A	HOH661

site_id	AC3
Number of Residues	4
Details	binding site for residue CL A 403

Chain	Residue
A	HIS16
A	LYS160
A	LYS238
B	ASP113

site_id	AC4
Number of Residues	22
Details	binding site for residue SAM B 401

Chain	Residue
A	ALA42
A	GLU57
A	GLN93
A	ASP96
A	ILE97
A	GLY112
A	ASP113
A	LYS262
A	HOH622
B	HIS16
B	PRO17
B	ASP158
B	LYS160
B	SER220
B	ARG222
B	PHE223
B	ASP231
B	HOH545
B	HOH550
B	HOH560
B	HOH611
B	HOH677

site_id	AC5
Number of Residues	16
Details	binding site for residue SAM B 402

Chain	Residue
B	ILE58
B	THR59
B	THR60
B	HIS61
B	ALA62
B	TYR63
B	VAL64
B	TRP71
B	GLU81
B	ASN82
B	VAL90
B	HOH507
B	HOH520
B	HOH551
B	HOH591
B	HOH660

site_id	AC6
Number of Residues	3
Details	binding site for residue CL B 403

Chain	Residue
B	HIS16
B	LYS160
B	LYS238

site_id	AC7
Number of Residues	20
Details	binding site for residue SAM E 401

Chain	Residue
F	HOH1229
E	HIS16
E	PRO17
E	ASP158
E	LYS160
E	SER220
E	ARG222
E	PHE223
E	ASP231
E	HOH520
E	HOH539
E	HOH577
F	GLU57
F	GLN93
F	ASP96
F	ILE97
F	GLY112
F	ASP113
F	LYS262
F	HOH1119

site_id	AC8
Number of Residues	20
Details	binding site for residue SAM E 402

Chain	Residue
A	ASN311
A	ASP314
A	GLU315
A	HOH719
E	ILE58
E	THR59
E	THR60
E	HIS61
E	ALA62
E	TYR63
E	VAL64
E	VAL90
E	HOH522
E	HOH531
E	HOH599
E	HOH628
E	HOH639
H	TRP71
H	GLU81
H	ASN82

site_id	AC9
Number of Residues	4
Details	binding site for residue CL E 403

Chain	Residue
E	HIS16
E	LYS160
E	LYS238
E	HOH720

site_id	AD1
Number of Residues	21
Details	binding site for residue SAM F 401

Chain	Residue
E	GLU57
E	GLN93
E	ASP96
E	ILE97
E	GLY112
E	ASP113
E	LYS262
E	HOH537
E	HOH615
F	HIS16
F	PRO17
F	ASP158
F	LYS160
F	SER220
F	ARG222
F	PHE223
F	ASP231
F	CL403
F	HOH1141
F	HOH1157
F	HOH1176

site_id	AD2
Number of Residues	11
Details	binding site for residue SAM F 402

Chain	Residue
F	ILE58
F	THR59
F	THR60
F	HIS61
F	ALA62
F	VAL64
F	VAL90
F	HOH1172
F	HOH1233
G	GLU81
G	ASN82

site_id	AD3
Number of Residues	4
Details	binding site for residue CL F 403

Chain	Residue
F	HIS16
F	LYS160
F	LYS238
F	SAM401

site_id	AD4
Number of Residues	20
Details	binding site for residue SAM G 401

Chain	Residue
G	HIS16
G	PRO17
G	ASP158
G	LYS160
G	SER220
G	ARG222
G	PHE223
G	ASP231
G	HOH522
G	HOH550
G	HOH571
G	HOH586
H	GLU57
H	GLN93
H	ASP96
H	ILE97
H	GLY112
H	ASP113
H	LYS262
H	HOH603

site_id	AD5
Number of Residues	15
Details	binding site for residue SAM G 402

Chain	Residue
F	TRP71
F	GLU81
F	ASN82
G	ILE58
G	THR59
G	THR60
G	HIS61
G	ALA62
G	TYR63
G	VAL64
G	VAL90
G	HOH533
G	HOH549
G	HOH583
G	HOH621

site_id	AD6
Number of Residues	3
Details	binding site for residue CL G 403

Chain	Residue
G	HIS16
G	LYS160
G	LYS238

site_id	AD7
Number of Residues	20
Details	binding site for residue SAM H 401

Chain	Residue
G	GLU57
G	GLN93
G	ASP96
G	ILE97
G	GLY112
G	ASP113
G	LYS262
H	HIS16
H	PRO17
H	ASP158
H	LYS160
H	SER220
H	ARG222
H	PHE223
H	ASP231
H	HOH523
H	HOH535
H	HOH541
H	HOH564
H	HOH623

site_id	AD8
Number of Residues	15
Details	binding site for residue SAM H 402

Chain	Residue
E	TRP71
E	GLU81
E	ASN82
H	ILE58
H	THR59
H	THR60
H	HIS61
H	ALA62
H	TYR63
H	VAL64
H	VAL90
H	HOH569
H	HOH587
H	HOH590
H	HOH606

site_id	AD9
Number of Residues	4
Details	binding site for residue CL H 403

Chain	Residue
G	ASP113
H	HIS16
H	LYS160
H	LYS238

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY110-TYR120

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

Chain	Residue	Details
A	GLY251-ASP259

246031

PDB entries from 2025-12-10

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