Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6S83

Crystal structure of methionine adenosyltransferase from Pyrococcus furiosus in complex with AMPPCP, SAM, and PCP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004478	molecular_function	methionine adenosyltransferase activity
A	0005524	molecular_function	ATP binding
A	0006556	biological_process	S-adenosylmethionine biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0016740	molecular_function	transferase activity
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0004478	molecular_function	methionine adenosyltransferase activity
B	0005524	molecular_function	ATP binding
B	0006556	biological_process	S-adenosylmethionine biosynthetic process
B	0006730	biological_process	one-carbon metabolic process
B	0016740	molecular_function	transferase activity
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0004478	molecular_function	methionine adenosyltransferase activity
C	0005524	molecular_function	ATP binding
C	0006556	biological_process	S-adenosylmethionine biosynthetic process
C	0006730	biological_process	one-carbon metabolic process
C	0016740	molecular_function	transferase activity
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0004478	molecular_function	methionine adenosyltransferase activity
D	0005524	molecular_function	ATP binding
D	0006556	biological_process	S-adenosylmethionine biosynthetic process
D	0006730	biological_process	one-carbon metabolic process
D	0016740	molecular_function	transferase activity
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0004478	molecular_function	methionine adenosyltransferase activity
E	0005524	molecular_function	ATP binding
E	0006556	biological_process	S-adenosylmethionine biosynthetic process
E	0006730	biological_process	one-carbon metabolic process
E	0016740	molecular_function	transferase activity
F	0000166	molecular_function	nucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0004478	molecular_function	methionine adenosyltransferase activity
F	0005524	molecular_function	ATP binding
F	0006556	biological_process	S-adenosylmethionine biosynthetic process
F	0006730	biological_process	one-carbon metabolic process
F	0016740	molecular_function	transferase activity
G	0000166	molecular_function	nucleotide binding
G	0000287	molecular_function	magnesium ion binding
G	0004478	molecular_function	methionine adenosyltransferase activity
G	0005524	molecular_function	ATP binding
G	0006556	biological_process	S-adenosylmethionine biosynthetic process
G	0006730	biological_process	one-carbon metabolic process
G	0016740	molecular_function	transferase activity
H	0000166	molecular_function	nucleotide binding
H	0000287	molecular_function	magnesium ion binding
H	0004478	molecular_function	methionine adenosyltransferase activity
H	0005524	molecular_function	ATP binding
H	0006556	biological_process	S-adenosylmethionine biosynthetic process
H	0006730	biological_process	one-carbon metabolic process
H	0016740	molecular_function	transferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue MDN A 501

Chain	Residue
A	LYS26
A	HOH625
B	ASP63
B	ASP159
B	GLU303
B	LYS308
B	HIS313
B	PO4501
B	MG502
B	MG503
B	HOH602
A	HIS30
B	HOH626
A	ASP32
A	LYS200
A	ARG286
A	MG502
A	SAM503
A	HOH603
A	HOH612

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 502

Chain	Residue
A	ASP32
A	MDN501
A	HOH607
A	HOH625
B	PO4501

site_id	AC3
Number of Residues	19
Details	binding site for residue SAM A 503

Chain	Residue
A	HIS30
A	PRO31
A	ASP198
A	LYS200
A	ALA215
A	ALA259
A	TYR268
A	SER275
A	GLY279
A	ASP280
A	MDN501
A	HOH614
B	HIS59
B	ASN61
B	ASP141
B	LEU142
B	ASN158
B	ASP159
B	HOH637

site_id	AC4
Number of Residues	5
Details	binding site for residue MG A 504

Chain	Residue
A	ASP159
B	ACP504
B	HOH621
B	HOH634
B	HOH657

site_id	AC5
Number of Residues	11
Details	binding site for residue PO4 B 501

Chain	Residue
A	LYS26
A	ASP32
A	ARG286
A	MDN501
A	MG502
A	HOH607
B	MET302
B	GLU303
B	ALA304
B	LYS308
B	MG502

site_id	AC6
Number of Residues	4
Details	binding site for residue MG B 502

Chain	Residue
A	MDN501
B	GLU303
B	PO4501
B	HOH626

site_id	AC7
Number of Residues	7
Details	binding site for residue MG B 503

Chain	Residue
A	ARG286
A	MDN501
A	HOH603
A	HOH612
B	ASP63
B	GLN64
B	HOH636

site_id	AC8
Number of Residues	25
Details	binding site for residue ACP B 504

Chain	Residue
A	HIS313
A	MG504
B	LYS26
B	HIS30
B	PRO31
B	ASP32
B	ASP198
B	LYS200
B	ALA215
B	TYR268
B	SER275
B	ASP280
B	PO4505
B	MG506
B	MG507
B	HOH605
B	HOH611
B	HOH619
B	HOH621
B	HOH632
B	HOH634
B	HOH642
B	HOH651
B	HOH655
B	HOH657

site_id	AC9
Number of Residues	13
Details	binding site for residue PO4 B 505

Chain	Residue
A	LYS308
B	LYS26
B	ASP32
B	ARG286
B	ACP504
B	MG506
B	HOH609
B	HOH611
B	HOH614
B	HOH619
A	MET302
A	GLU303
A	ALA304

site_id	AD1
Number of Residues	6
Details	binding site for residue MG B 506

Chain	Residue
B	ASP32
B	ACP504
B	PO4505
B	HOH611
B	HOH614
B	HOH642

site_id	AD2
Number of Residues	6
Details	binding site for residue MG B 507

Chain	Residue
B	GLU24
B	ACP504
B	HOH603
B	HOH619
B	HOH632
B	HOH647

site_id	AD3
Number of Residues	19
Details	binding site for residue MDN C 501

Chain	Residue
C	LYS26
C	HIS30
C	ASP32
C	LYS200
C	PO4502
C	MG503
C	HOH601
C	HOH603
C	HOH606
C	HOH618
C	HOH634
D	ASP63
D	ASP159
D	GLU303
D	LYS308
D	HIS313
D	MG501
D	MG502
D	HOH632

site_id	AD4
Number of Residues	11
Details	binding site for residue PO4 C 502

Chain	Residue
C	LYS26
C	ASP32
C	ARG286
C	MDN501
C	MG503
C	HOH606
D	MET302
D	GLU303
D	ALA304
D	LYS308
D	MG501

site_id	AD5
Number of Residues	5
Details	binding site for residue MG C 503

Chain	Residue
C	ASP32
C	MDN501
C	PO4502
C	HOH606
C	HOH618

site_id	AD6
Number of Residues	4
Details	binding site for residue MG D 501

Chain	Residue
C	MDN501
C	PO4502
D	GLU303
D	HOH632

site_id	AD7
Number of Residues	7
Details	binding site for residue MG D 502

Chain	Residue
C	ARG286
C	MDN501
C	HOH601
C	HOH634
D	ASP63
D	GLN64
D	HOH647

site_id	AD8
Number of Residues	23
Details	binding site for residue ACP D 503

Chain	Residue
C	HIS313
D	LYS26
D	HIS30
D	PRO31
D	ASP32
D	ASP198
D	LYS200
D	ALA215
D	TYR268
D	SER275
D	ASP280
D	PO4504
D	MG505
D	MG506
D	HOH604
D	HOH613
D	HOH621
D	HOH625
D	HOH629
D	HOH631
D	HOH636
D	HOH652
D	HOH657

site_id	AD9
Number of Residues	13
Details	binding site for residue PO4 D 504

Chain	Residue
C	GLU303
C	ALA304
C	LYS308
D	LYS26
D	ASP32
D	ARG286
D	ACP503
D	MG505
D	MG506
D	HOH608
D	HOH619
D	HOH621
D	HOH657

site_id	AE1
Number of Residues	6
Details	binding site for residue MG D 505

Chain	Residue
D	ASP32
D	ACP503
D	PO4504
D	HOH619
D	HOH629
D	HOH657

site_id	AE2
Number of Residues	7
Details	binding site for residue MG D 506

Chain	Residue
D	GLU24
D	ACP503
D	PO4504
D	HOH604
D	HOH621
D	HOH633
D	HOH667

site_id	AE3
Number of Residues	19
Details	binding site for residue MDN E 501

Chain	Residue
E	LYS26
E	HIS30
E	ASP32
E	LYS200
E	MG502
E	SAM503
E	HOH604
E	HOH605
E	HOH621
F	ASP63
F	ASP159
F	GLU303
F	LYS308
F	HIS313
F	PO4501
F	MG502
F	MG503
F	HOH605
F	HOH612

site_id	AE4
Number of Residues	6
Details	binding site for residue MG E 502

Chain	Residue
E	ASP32
E	MDN501
E	HOH605
E	HOH621
F	PO4501
F	MG503

site_id	AE5
Number of Residues	21
Details	binding site for residue SAM E 503

Chain	Residue
E	HIS30
E	PRO31
E	ASP198
E	LYS200
E	ALA215
E	ALA259
E	TYR268
E	SER275
E	GLY279
E	ASP280
E	MDN501
E	HOH604
E	HOH613
E	HOH614
F	HIS59
F	ASN61
F	ASP141
F	LEU142
F	ASN158
F	ASP159
F	ILE346

site_id	AE6
Number of Residues	11
Details	binding site for residue PO4 F 501

Chain	Residue
E	LYS26
E	ASP32
E	ARG286
E	MDN501
E	MG502
F	ASP63
F	MET302
F	GLU303
F	ALA304
F	LYS308
F	MG502

site_id	AE7
Number of Residues	4
Details	binding site for residue MG F 502

Chain	Residue
E	MDN501
F	GLU303
F	PO4501
F	HOH605

site_id	AE8
Number of Residues	8
Details	binding site for residue MG F 503

Chain	Residue
E	ASP281
E	MDN501
E	MG502
E	HOH604
E	HOH621
F	ASP63
F	GLN64
F	HOH647

site_id	AE9
Number of Residues	22
Details	binding site for residue ACP F 504

Chain	Residue
E	HIS313
E	HOH615
F	LYS26
F	HIS30
F	PRO31
F	ASP32
F	ASP198
F	LYS200
F	ALA215
F	TYR268
F	SER275
F	ASP280
F	PO4505
F	MG506
F	MG507
F	HOH625
F	HOH627
F	HOH634
F	HOH636
F	HOH640
F	HOH641
F	HOH642

site_id	AF1
Number of Residues	12
Details	binding site for residue PO4 F 505

Chain	Residue
E	GLU303
E	ALA304
E	LYS308
E	HOH615
F	LYS26
F	ASP32
F	ARG286
F	ACP504
F	MG506
F	HOH609
F	HOH642
F	HOH643

site_id	AF2
Number of Residues	6
Details	binding site for residue MG F 506

Chain	Residue
F	ASP32
F	ACP504
F	PO4505
F	HOH615
F	HOH625
F	HOH642

site_id	AF3
Number of Residues	7
Details	binding site for residue MG F 507

Chain	Residue
E	HOH615
F	GLU24
F	LYS200
F	ACP504
F	HOH601
F	HOH610
F	HOH636

site_id	AF4
Number of Residues	11
Details	binding site for residue PO4 G 501

Chain	Residue
G	LYS26
G	ASP32
G	ARG286
G	MG502
G	HOH604
H	MET302
H	GLU303
H	ALA304
H	LYS308
H	MDN501
H	MG502

site_id	AF5
Number of Residues	5
Details	binding site for residue MG G 502

Chain	Residue
G	ASP32
G	PO4501
G	HOH604
G	HOH620
H	MDN501

site_id	AF6
Number of Residues	18
Details	binding site for residue MDN H 501

Chain	Residue
G	LYS26
G	HIS30
G	ASP32
G	LYS200
G	PO4501
G	MG502
G	HOH620
H	ASP63
H	ASP159
H	GLU303
H	LYS308
H	HIS313
H	MG502
H	MG503
H	HOH608
H	HOH611
H	HOH617
H	HOH630

site_id	AF7
Number of Residues	5
Details	binding site for residue MG H 502

Chain	Residue
G	PO4501
H	SER161
H	GLU303
H	MDN501
H	HOH611

site_id	AF8
Number of Residues	7
Details	binding site for residue MG H 503

Chain	Residue
G	ARG286
H	ASP63
H	GLN64
H	MDN501
H	HOH608
H	HOH630
H	HOH635

site_id	AF9
Number of Residues	19
Details	binding site for residue ACP H 504

Chain	Residue
G	GLU303
G	HIS313
G	HOH601
H	LYS26
H	HIS30
H	PRO31
H	ASP32
H	ASP198
H	LYS200
H	ALA215
H	TYR268
H	SER275
H	ASP280
H	PO4505
H	MG506
H	MG507
H	HOH602
H	HOH605
H	HOH610

site_id	AG1
Number of Residues	13
Details	binding site for residue PO4 H 505

Chain	Residue
G	MET302
G	GLU303
G	ALA304
G	LYS308
H	LYS26
H	ASP32
H	ARG286
H	ACP504
H	MG506
H	MG507
H	HOH605
H	HOH619
H	HOH632

site_id	AG2
Number of Residues	6
Details	binding site for residue MG H 506

Chain	Residue
H	ASP32
H	ACP504
H	PO4505
H	HOH610
H	HOH619
H	HOH632

site_id	AG3
Number of Residues	5
Details	binding site for residue MG H 507

Chain	Residue
H	GLU24
H	ACP504
H	PO4505
H	HOH602
H	HOH605

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00136","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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