1JNR

Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6 resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000104	molecular_function	succinate dehydrogenase activity
A	0000166	molecular_function	nucleotide binding
A	0005886	cellular_component	plasma membrane
A	0009055	molecular_function	electron transfer activity
A	0009061	biological_process	anaerobic respiration
A	0016491	molecular_function	oxidoreductase activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0000104	molecular_function	succinate dehydrogenase activity
C	0000166	molecular_function	nucleotide binding
C	0005886	cellular_component	plasma membrane
C	0009055	molecular_function	electron transfer activity
C	0009061	biological_process	anaerobic respiration
C	0016491	molecular_function	oxidoreductase activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD A 1000

Chain	Residue
A	GLY29
A	ALA65
A	VAL66
A	LEU70
A	ALA72
A	ILE73
A	ASN74
A	PHE175
A	ILE176
A	ALA213
A	THR214
A	GLY30
A	GLY215
A	TRP234
A	TYR235
A	ALA236
A	ASP239
A	SER242
A	MET365
A	SER397
A	GLY438
A	ASP439
A	GLY31
A	PHE448
A	SER449
A	SER452
A	HOH5045
A	HOH5121
A	HOH5316
A	HOH5321
A	HOH5718
A	HOH7001
A	HOH7002
A	PHE32
A	SER33
A	GLU56
A	LYS57
A	SER63
A	GLY64

---

site_id	AC2
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD C 3000

Chain	Residue
C	GLY29
C	GLY30
C	GLY31
C	PHE32
C	SER33
C	GLU56
C	LYS57
C	SER63
C	GLY64
C	ALA65
C	VAL66
C	LEU70
C	ALA72
C	ILE73
C	ASN74
C	PHE175
C	ILE176
C	ALA213
C	THR214
C	GLY215
C	TRP234
C	TYR235
C	ALA236
C	ASP239
C	SER242
C	MET365
C	SER397
C	GLY438
C	ASP439
C	PHE448
C	SER449
C	SER452
C	HOH5008
C	HOH5048
C	HOH5059
C	HOH5197
C	HOH5320
C	HOH5621
C	HOH7057

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 1100

Chain	Residue
B	SER3
B	CYS25
B	ASN41
B	CYS47
B	TRP48
B	CYS50
B	TYR51
B	CYS53

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 1110

Chain	Residue
B	CYS10
B	ASP11
B	GLY12
B	CYS13
B	THR19
B	ALA20
B	CYS21
B	CYS57
B	ILE62

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 D 3100

Chain	Residue
D	CYS47
D	TRP48
D	CYS50
D	TYR51
D	CYS53
D	SER3
D	CYS25
D	PRO26
D	ASN41

---

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 D 3110

Chain	Residue
D	CYS10
D	ASP11
D	GLY12
D	CYS13
D	THR19
D	ALA20
D	CYS21
D	ALA39
D	CYS57
D	ILE62

---

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 6501

Chain	Residue
C	LYS181
C	ALA250
C	LYS620
C	ASP622
C	ALA623
C	GLU624
C	HOH5074
C	HOH5198
C	HOH5865
C	HOH7015

---

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 6503

Chain	Residue
A	LYS267
A	ASP268
A	LEU372
A	GLN376
A	GLU386
A	HOH5263
A	HOH5753
C	TYR528
C	ARG545
C	LEU549

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 6504

Chain	Residue
C	PHE264
C	TYR292
C	ARG317
C	ASN318
C	VAL321
C	HOH6090

---

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 6505

Chain	Residue
A	TYR528
A	ARG545
A	LEU549
C	LYS267
C	ASP268
C	LEU372
C	GLN376
C	GLU386
C	HOH5642

---

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CwECYsCVkMCP

Chain	Residue	Details
B	CYS47-PRO58

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	9
Details	a catalytic site defined by CSA, PubMed 11842205, 16503650

Chain	Residue	Details
A	ASP361
A	TRP234
A	SER449
A	SER449
A	ASN74
A	GLU141
A	ARG265
A	HIS398
B	TRP48

---

site_id	CSA2
Number of Residues	7
Details	a catalytic site defined by CSA, PubMed 11842205, 16503650

Chain	Residue	Details
C	TRP234
C	ASP361
C	SER449
C	ASN74
C	ARG265
C	GLU141
C	HIS398

---

site_id	CSA3
Number of Residues	9
Details	a catalytic site defined by CSA, PubMed 11842205, 16503650

Chain	Residue	Details
A	ASP361
A	TRP234
A	SER449
A	SER449
A	ASN74
A	GLU141
A	ARG265
A	HIS398
B	TRP48

---

site_id	CSA4
Number of Residues	7
Details	a catalytic site defined by CSA, PubMed 11842205, 16503650

Chain	Residue	Details
C	TRP234
C	ASP361
C	ASN74
C	ARG265
C	GLU141
C	HIS398
D	TRP48

---

site_id	MCSA1
Number of Residues	1
Details	M-CSA 123

Chain	Residue	Details
B	TRP48	single electron acceptor, single electron donor, single electron relay, van der waals interaction
A	GLU141	activator, hydrogen bond acceptor
A	TRP234	hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity
A	ARG265	electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
A	ASP361	activator, hydrogen bond acceptor
A	HIS398	electrostatic stabiliser, hydrogen bond donor
A	SER449	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA2
Number of Residues	1
Details	M-CSA 123

Chain	Residue	Details
D	TRP48	single electron acceptor, single electron donor, single electron relay, van der waals interaction
C	GLU141	activator, hydrogen bond acceptor
C	TRP234	hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity
C	ARG265	electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
C	ASP361	activator, hydrogen bond acceptor
C	HIS398	electrostatic stabiliser, hydrogen bond donor
C	SER449	electrostatic stabiliser, hydrogen bond donor

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