Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VDC

THE 9.5 A RESOLUTION STRUCTURE OF GLUTAMATE SYNTHASE FROM CRYO-ELECTRON MICROSCOPY AND ITS OLIGOMERIZATION BEHAVIOR IN SOLUTION: FUNCTIONAL IMPLICATIONS.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004355	molecular_function	glutamate synthase (NADPH) activity
A	0006537	biological_process	glutamate biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0015930	molecular_function	glutamate synthase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
A	0019676	biological_process	ammonia assimilation cycle
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051538	molecular_function	3 iron, 4 sulfur cluster binding
A	0097054	biological_process	L-glutamate biosynthetic process
B	0004355	molecular_function	glutamate synthase (NADPH) activity
B	0006537	biological_process	glutamate biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0015930	molecular_function	glutamate synthase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
B	0019676	biological_process	ammonia assimilation cycle
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051538	molecular_function	3 iron, 4 sulfur cluster binding
B	0097054	biological_process	L-glutamate biosynthetic process
C	0004355	molecular_function	glutamate synthase (NADPH) activity
C	0006537	biological_process	glutamate biosynthetic process
C	0008652	biological_process	amino acid biosynthetic process
C	0015930	molecular_function	glutamate synthase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
C	0019676	biological_process	ammonia assimilation cycle
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051538	molecular_function	3 iron, 4 sulfur cluster binding
C	0097054	biological_process	L-glutamate biosynthetic process
D	0004355	molecular_function	glutamate synthase (NADPH) activity
D	0006537	biological_process	glutamate biosynthetic process
D	0008652	biological_process	amino acid biosynthetic process
D	0015930	molecular_function	glutamate synthase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
D	0019676	biological_process	ammonia assimilation cycle
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051538	molecular_function	3 iron, 4 sulfur cluster binding
D	0097054	biological_process	L-glutamate biosynthetic process
E	0004355	molecular_function	glutamate synthase (NADPH) activity
E	0006537	biological_process	glutamate biosynthetic process
E	0008652	biological_process	amino acid biosynthetic process
E	0015930	molecular_function	glutamate synthase activity
E	0016491	molecular_function	oxidoreductase activity
E	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
E	0019676	biological_process	ammonia assimilation cycle
E	0046872	molecular_function	metal ion binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051538	molecular_function	3 iron, 4 sulfur cluster binding
E	0097054	biological_process	L-glutamate biosynthetic process
F	0004355	molecular_function	glutamate synthase (NADPH) activity
F	0006537	biological_process	glutamate biosynthetic process
F	0008652	biological_process	amino acid biosynthetic process
F	0015930	molecular_function	glutamate synthase activity
F	0016491	molecular_function	oxidoreductase activity
F	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
F	0019676	biological_process	ammonia assimilation cycle
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051538	molecular_function	3 iron, 4 sulfur cluster binding
F	0097054	biological_process	L-glutamate biosynthetic process
G	0004355	molecular_function	glutamate synthase (NADPH) activity
G	0006537	biological_process	glutamate biosynthetic process
G	0008652	biological_process	amino acid biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0097054	biological_process	L-glutamate biosynthetic process
H	0004355	molecular_function	glutamate synthase (NADPH) activity
H	0006537	biological_process	glutamate biosynthetic process
H	0008652	biological_process	amino acid biosynthetic process
H	0016491	molecular_function	oxidoreductase activity
H	0046872	molecular_function	metal ion binding
H	0051536	molecular_function	iron-sulfur cluster binding
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding
H	0097054	biological_process	L-glutamate biosynthetic process
I	0004355	molecular_function	glutamate synthase (NADPH) activity
I	0006537	biological_process	glutamate biosynthetic process
I	0008652	biological_process	amino acid biosynthetic process
I	0016491	molecular_function	oxidoreductase activity
I	0046872	molecular_function	metal ion binding
I	0051536	molecular_function	iron-sulfur cluster binding
I	0051539	molecular_function	4 iron, 4 sulfur cluster binding
I	0097054	biological_process	L-glutamate biosynthetic process
J	0004355	molecular_function	glutamate synthase (NADPH) activity
J	0006537	biological_process	glutamate biosynthetic process
J	0008652	biological_process	amino acid biosynthetic process
J	0016491	molecular_function	oxidoreductase activity
J	0046872	molecular_function	metal ion binding
J	0051536	molecular_function	iron-sulfur cluster binding
J	0051539	molecular_function	4 iron, 4 sulfur cluster binding
J	0097054	biological_process	L-glutamate biosynthetic process
K	0004355	molecular_function	glutamate synthase (NADPH) activity
K	0006537	biological_process	glutamate biosynthetic process
K	0008652	biological_process	amino acid biosynthetic process
K	0016491	molecular_function	oxidoreductase activity
K	0046872	molecular_function	metal ion binding
K	0051536	molecular_function	iron-sulfur cluster binding
K	0051539	molecular_function	4 iron, 4 sulfur cluster binding
K	0097054	biological_process	L-glutamate biosynthetic process
L	0004355	molecular_function	glutamate synthase (NADPH) activity
L	0006537	biological_process	glutamate biosynthetic process
L	0008652	biological_process	amino acid biosynthetic process
L	0016491	molecular_function	oxidoreductase activity
L	0046872	molecular_function	metal ion binding
L	0051536	molecular_function	iron-sulfur cluster binding
L	0051539	molecular_function	4 iron, 4 sulfur cluster binding
L	0097054	biological_process	L-glutamate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OMT A 2473

Chain	Residue
A	CYS1
A	ARG210
A	TYR211
A	GLN223
A	ASN231
A	GLY232
A	GLU233
A	ASP273
A	SER274

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE FMN A 2474

Chain	Residue
A	PRO856
A	GLY857
A	MET858
A	SER859
A	GLY885
A	GLU886
A	GLN909
A	LYS931
A	LYS999
A	GLY1028
A	GLY1029
A	THR1030
A	GLY1031
A	ASP1070
A	GLY1071
A	GLY1072
A	GLY1093
A	THR1094
A	AKG2475

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AKG A 2475

Chain	Residue
A	SER859
A	GLN934
A	LYS937
A	GLY942
A	GLN943
A	ARG957
A	THR1030
A	GLY1031
A	FMN2474

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S A 2476

Chain	Residue
A	CYS1102
A	ILE1103
A	MET1104
A	VAL1105
A	ARG1106
A	GLN1107
A	CYS1108
A	CYS1113
A	VAL1117
A	CYS1118

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OMT B 2473

Chain	Residue
B	CYS1
B	GLN209
B	ARG210
B	TYR211
B	GLN223
B	ASN231
B	GLY232
B	GLU233
B	ASP273
B	SER274

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN B 2474

Chain	Residue
B	PRO856
B	GLY857
B	MET858
B	SER859
B	GLU886
B	GLN909
B	LYS931
B	LYS999
B	GLY1028
B	GLY1029
B	THR1030
B	GLY1031
B	ASP1070
B	GLY1071
B	GLY1072
B	GLY1093
B	THR1094
B	AKG2475

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AKG B 2475

Chain	Residue
B	SER859
B	GLN934
B	LYS937
B	GLY942
B	GLN943
B	ARG957
B	THR1030
B	GLY1031
B	ALA1032
B	FMN2474

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S B 2476

Chain	Residue
B	CYS1102
B	ILE1103
B	MET1104
B	VAL1105
B	ARG1106
B	GLN1107
B	CYS1108
B	CYS1113
B	VAL1117
B	CYS1118

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OMT C 2473

Chain	Residue
C	ASN231
C	GLY232
C	GLU233
C	ASP273
C	SER274
C	CYS1
C	ARG210
C	TYR211
C	GLN223

site_id	BC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE FMN C 2474

Chain	Residue
C	PRO856
C	GLY857
C	MET858
C	SER859
C	GLY885
C	GLU886
C	GLN909
C	LYS931
C	LYS999
C	GLY1028
C	GLY1029
C	THR1030
C	GLY1031
C	ASP1070
C	GLY1071
C	GLY1072
C	GLY1093
C	THR1094
C	AKG2475

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AKG C 2475

Chain	Residue
C	SER859
C	GLN934
C	LYS937
C	GLY942
C	GLN943
C	ARG957
C	THR1030
C	GLY1031
C	FMN2474

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S C 2476

Chain	Residue
C	CYS1102
C	ILE1103
C	MET1104
C	VAL1105
C	ARG1106
C	GLN1107
C	CYS1108
C	CYS1113
C	VAL1117
C	CYS1118

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OMT D 2473

Chain	Residue
D	CYS1
D	GLN209
D	ARG210
D	TYR211
D	GLN223
D	ASN231
D	GLY232
D	GLU233
D	ASP273
D	SER274

site_id	BC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN D 2474

Chain	Residue
D	PRO856
D	GLY857
D	MET858
D	SER859
D	GLU886
D	GLN909
D	LYS931
D	LYS999
D	GLY1028
D	GLY1029
D	THR1030
D	GLY1031
D	ASP1070
D	GLY1071
D	GLY1072
D	GLY1093
D	THR1094
D	AKG2475

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AKG D 2475

Chain	Residue
D	SER859
D	GLN934
D	LYS937
D	GLY942
D	GLN943
D	ARG957
D	THR1030
D	GLY1031
D	ALA1032
D	FMN2474

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S D 2476

Chain	Residue
D	CYS1102
D	ILE1103
D	MET1104
D	VAL1105
D	ARG1106
D	GLN1107
D	CYS1108
D	CYS1113
D	VAL1117
D	CYS1118

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OMT E 2473

Chain	Residue
E	CYS1
E	ARG210
E	TYR211
E	GLN223
E	ASN231
E	GLY232
E	GLU233
E	ASP273
E	SER274

site_id	BC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE FMN E 2474

Chain	Residue
E	PRO856
E	GLY857
E	MET858
E	SER859
E	GLY885
E	GLU886
E	GLN909
E	LYS931
E	LYS999
E	GLY1028
E	GLY1029
E	THR1030
E	GLY1031
E	ASP1070
E	GLY1071
E	GLY1072
E	GLY1093
E	THR1094
E	AKG2475

site_id	CC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AKG E 2475

Chain	Residue
E	SER859
E	GLN934
E	LYS937
E	GLY942
E	GLN943
E	ARG957
E	THR1030
E	GLY1031
E	FMN2474

site_id	CC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S E 2476

Chain	Residue
E	CYS1102
E	ILE1103
E	MET1104
E	VAL1105
E	ARG1106
E	GLN1107
E	CYS1108
E	CYS1113
E	VAL1117
E	CYS1118

site_id	CC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OMT F 2473

Chain	Residue
F	CYS1
F	GLN209
F	ARG210
F	TYR211
F	GLN223
F	ASN231
F	GLY232
F	GLU233
F	ASP273
F	SER274

site_id	CC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN F 2474

Chain	Residue
F	PRO856
F	GLY857
F	MET858
F	SER859
F	GLU886
F	GLN909
F	LYS931
F	LYS999
F	GLY1028
F	GLY1029
F	THR1030
F	GLY1031
F	ASP1070
F	GLY1071
F	GLY1072
F	GLY1093
F	THR1094
F	AKG2475

site_id	CC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AKG F 2475

Chain	Residue
F	SER859
F	GLN934
F	LYS937
F	GLY942
F	GLN943
F	ARG957
F	THR1030
F	GLY1031
F	ALA1032
F	FMN2474

site_id	CC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S F 2476

Chain	Residue
F	CYS1102
F	ILE1103
F	MET1104
F	VAL1105
F	ARG1106
F	GLN1107
F	CYS1108
F	CYS1113
F	VAL1117
F	CYS1118

site_id	CC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 G 482

Chain	Residue
G	CYS59
G	ILE65
G	ASN88
G	CYS98
G	GLN100
G	LEU103
G	CYS104
G	GLU124

site_id	CC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 G 483

Chain	Residue
G	CYS47
G	SER48
G	CYS50
G	CYS55
G	CYS108
G	VAL109
G	ILE110
G	VAL118
G	ILE120

site_id	CC9
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD G 484

Chain	Residue
G	ILE97
G	ILE153
G	GLY154
G	GLY156
G	PRO157
G	ALA158
G	ASP177
G	ARG178
G	TYR179
G	GLY184
G	LEU185
G	LYS194
G	GLU219
G	VAL220
G	ALA239
G	THR240
G	GLY241
G	LEU265
G	ASP299
G	THR300
G	ASP303
G	ASN408
G	GLY441
G	ASP442
G	SER448
G	LEU449
G	VAL450
G	ALA453

site_id	DC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 H 482

Chain	Residue
H	CYS59
H	ILE65
H	ASN88
H	CYS98
H	GLN100
H	LEU103
H	CYS104
H	GLU124

site_id	DC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 H 483

Chain	Residue
H	CYS47
H	SER48
H	CYS50
H	CYS55
H	CYS108
H	VAL109
H	ILE110
H	VAL118
H	ILE120

site_id	DC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD H 484

Chain	Residue
H	ILE97
H	ILE153
H	GLY154
H	GLY156
H	PRO157
H	ALA158
H	ASP177
H	ARG178
H	TYR179
H	GLY184
H	LEU185
H	LYS194
H	GLU219
H	VAL220
H	ALA239
H	THR240
H	GLY241
H	LEU265
H	ASP299
H	THR300
H	ASP303
H	ASN408
H	GLY441
H	ASP442
H	SER448
H	LEU449
H	VAL450
H	ALA453

site_id	DC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 I 482

Chain	Residue
I	CYS59
I	ILE65
I	ASN88
I	CYS98
I	GLN100
I	LEU103
I	CYS104
I	GLU124

site_id	DC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 I 483

Chain	Residue
I	CYS47
I	SER48
I	CYS50
I	CYS55
I	CYS108
I	VAL109
I	ILE110
I	VAL118
I	ILE120

site_id	DC6
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD I 484

Chain	Residue
I	ILE97
I	ILE153
I	GLY154
I	GLY156
I	PRO157
I	ALA158
I	ASP177
I	ARG178
I	TYR179
I	GLY184
I	LEU185
I	LYS194
I	GLU219
I	VAL220
I	ALA239
I	THR240
I	GLY241
I	LEU265
I	ASP299
I	THR300
I	ASP303
I	ASN408
I	GLY441
I	ASP442
I	SER448
I	LEU449
I	VAL450
I	ALA453

site_id	DC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 J 482

Chain	Residue
J	CYS59
J	ILE65
J	ASN88
J	CYS98
J	GLN100
J	LEU103
J	CYS104
J	GLU124

site_id	DC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 J 483

Chain	Residue
J	CYS47
J	SER48
J	CYS50
J	CYS55
J	CYS108
J	VAL109
J	ILE110
J	VAL118
J	ILE120

site_id	DC9
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD J 484

Chain	Residue
J	ILE97
J	ILE153
J	GLY154
J	GLY156
J	PRO157
J	ALA158
J	ASP177
J	ARG178
J	TYR179
J	GLY184
J	LEU185
J	LYS194
J	GLU219
J	VAL220
J	ALA239
J	THR240
J	GLY241
J	LEU265
J	ASP299
J	THR300
J	ASP303
J	ASN408
J	GLY441
J	ASP442
J	SER448
J	LEU449
J	VAL450
J	ALA453

site_id	EC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 K 482

Chain	Residue
K	CYS59
K	ILE65
K	ASN88
K	CYS98
K	GLN100
K	LEU103
K	CYS104
K	GLU124

site_id	EC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 K 483

Chain	Residue
K	CYS47
K	SER48
K	CYS50
K	CYS55
K	CYS108
K	VAL109
K	ILE110
K	VAL118
K	ILE120

site_id	EC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD K 484

Chain	Residue
K	ILE97
K	ILE153
K	GLY154
K	GLY156
K	PRO157
K	ALA158
K	ASP177
K	ARG178
K	TYR179
K	GLY184
K	LEU185
K	LYS194
K	GLU219
K	VAL220
K	ALA239
K	THR240
K	GLY241
K	LEU265
K	ASP299
K	THR300
K	ASP303
K	ASN408
K	GLY441
K	ASP442
K	SER448
K	LEU449
K	VAL450
K	ALA453

site_id	EC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 L 482

Chain	Residue
L	CYS59
L	ILE65
L	ASN88
L	CYS98
L	GLN100
L	LEU103
L	CYS104
L	GLU124

site_id	EC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 L 483

Chain	Residue
L	CYS47
L	SER48
L	CYS50
L	CYS55
L	CYS108
L	VAL109
L	ILE110
L	VAL118
L	ILE120

site_id	EC6
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD L 484

Chain	Residue
L	ILE97
L	ILE153
L	GLY154
L	GLY156
L	PRO157
L	ALA158
L	ASP177
L	ARG178
L	TYR179
L	GLY184
L	LEU185
L	LYS194
L	GLU219
L	VAL220
L	ALA239
L	THR240
L	GLY241
L	LEU265
L	ASP299
L	THR300
L	ASP303
L	ASN408
L	GLY441
L	ASP442
L	SER448
L	LEU449
L	VAL450
L	ALA453

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2370
Details	Domain: {"description":"Glutamine amidotransferase type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00609","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	126
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	60
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Active site: {"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	696
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	198
Details	Domain: {"description":"4Fe-4S ferredoxin-type"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ofd

Chain	Residue	Details
A	LYS937
A	GLU886
A	CYS1

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ofd

Chain	Residue	Details
B	LYS937
B	GLU886
B	CYS1

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ofd

Chain	Residue	Details
C	LYS937
C	GLU886
C	CYS1

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ofd

Chain	Residue	Details
D	LYS937
D	GLU886
D	CYS1

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1ofd

Chain	Residue	Details
E	LYS937
E	GLU886
E	CYS1

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ofd

Chain	Residue	Details
F	LYS937
F	GLU886
F	CYS1

site_id	MCSA1
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
A	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	ASN231	electrostatic stabiliser, hydrogen bond donor
A	GLY232	electrostatic stabiliser, hydrogen bond donor
A	MET479	single electron acceptor, single electron donor, single electron relay
A	GLU886	proton acceptor, proton donor, proton relay
A	LYS937	electrostatic stabiliser

site_id	MCSA2
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
B	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	ASN231	electrostatic stabiliser, hydrogen bond donor
B	GLY232	electrostatic stabiliser, hydrogen bond donor
B	MET479	single electron acceptor, single electron donor, single electron relay
B	GLU886	proton acceptor, proton donor, proton relay
B	LYS937	electrostatic stabiliser

site_id	MCSA3
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
C	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
C	ASN231	electrostatic stabiliser, hydrogen bond donor
C	GLY232	electrostatic stabiliser, hydrogen bond donor
C	MET479	single electron acceptor, single electron donor, single electron relay
C	GLU886	proton acceptor, proton donor, proton relay
C	LYS937	electrostatic stabiliser

site_id	MCSA4
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
D	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
D	ASN231	electrostatic stabiliser, hydrogen bond donor
D	GLY232	electrostatic stabiliser, hydrogen bond donor
D	MET479	single electron acceptor, single electron donor, single electron relay
D	GLU886	proton acceptor, proton donor, proton relay
D	LYS937	electrostatic stabiliser

site_id	MCSA5
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
E	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
E	ASN231	electrostatic stabiliser, hydrogen bond donor
E	GLY232	electrostatic stabiliser, hydrogen bond donor
E	MET479	single electron acceptor, single electron donor, single electron relay
E	GLU886	proton acceptor, proton donor, proton relay
E	LYS937	electrostatic stabiliser

site_id	MCSA6
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
F	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
F	ASN231	electrostatic stabiliser, hydrogen bond donor
F	GLY232	electrostatic stabiliser, hydrogen bond donor
F	MET479	single electron acceptor, single electron donor, single electron relay
F	GLU886	proton acceptor, proton donor, proton relay
F	LYS937	electrostatic stabiliser

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