6MO6

Crystal structure of the selenomethionine-substituted human sulfide:quinone oxidoreductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006790	biological_process	sulfur compound metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0048038	molecular_function	quinone binding
A	0070221	biological_process	sulfide oxidation, using sulfide:quinone oxidoreductase
A	0070224	molecular_function	sulfide:quinone oxidoreductase activity
A	0071949	molecular_function	FAD binding
A	0106436	molecular_function	glutathione-dependent sulfide quinone oxidoreductase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006790	biological_process	sulfur compound metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0048038	molecular_function	quinone binding
B	0070221	biological_process	sulfide oxidation, using sulfide:quinone oxidoreductase
B	0070224	molecular_function	sulfide:quinone oxidoreductase activity
B	0071949	molecular_function	FAD binding
B	0106436	molecular_function	glutathione-dependent sulfide quinone oxidoreductase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0006790	biological_process	sulfur compound metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0048038	molecular_function	quinone binding
C	0070221	biological_process	sulfide oxidation, using sulfide:quinone oxidoreductase
C	0070224	molecular_function	sulfide:quinone oxidoreductase activity
C	0071949	molecular_function	FAD binding
C	0106436	molecular_function	glutathione-dependent sulfide quinone oxidoreductase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005743	cellular_component	mitochondrial inner membrane
D	0006790	biological_process	sulfur compound metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0048038	molecular_function	quinone binding
D	0070221	biological_process	sulfide oxidation, using sulfide:quinone oxidoreductase
D	0070224	molecular_function	sulfide:quinone oxidoreductase activity
D	0071949	molecular_function	FAD binding
D	0106436	molecular_function	glutathione-dependent sulfide quinone oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	binding site for residue FAD A 501

Chain	Residue
A	GLY52
A	VAL118
A	LEU145
A	GLY146
A	ASN169
A	TYR170
A	CYS201
A	LYS207
A	GLY335
A	ASP336
A	LYS344
A	SER53
A	THR345
A	ALA346
A	ALA347
A	SER378
A	PRO380
A	LYS418
A	HOH609
A	HOH622
A	HOH627
A	GLY54
A	VAL74
A	GLU75
A	PRO76
A	GLN83
A	PRO84
A	ARG117

---

site_id	AC2
Number of Residues	1
Details	binding site for residue CL A 502

Chain	Residue
A	ARG61

---

site_id	AC3
Number of Residues	33
Details	binding site for residue FAD B 501

Chain	Residue
B	GLY50
B	GLY52
B	SER53
B	GLY54
B	GLU75
B	PRO76
B	GLN83
B	PRO84
B	THR87
B	ARG117
B	VAL118
B	LEU145
B	GLY146
B	ASN169
B	TYR170
B	CYS201
B	LYS207
B	GLY335
B	ASP336
B	LYS344
B	THR345
B	ALA346
B	ALA347
B	VAL349
B	SER378
B	CSS379
B	PRO380
B	LYS418
B	HOH601
B	HOH602
B	HOH605
B	HOH608
B	HOH621

---

site_id	AC4
Number of Residues	1
Details	binding site for residue CL B 502

Chain	Residue
B	ARG61

---

site_id	AC5
Number of Residues	33
Details	binding site for residue FAD C 501

Chain	Residue
C	GLY52
C	SER53
C	GLY54
C	VAL74
C	GLU75
C	PRO76
C	GLN83
C	PRO84
C	ARG117
C	VAL118
C	LEU145
C	GLY146
C	ASN169
C	TYR170
C	LYS200
C	CYS201
C	LYS207
C	GLY335
C	ASP336
C	LYS344
C	THR345
C	ALA346
C	ALA347
C	VAL349
C	SER378
C	CSS379
C	PRO380
C	LYS418
C	HOH611
C	HOH623
C	HOH627
C	HOH632
C	HOH640

---

site_id	AC6
Number of Residues	1
Details	binding site for residue CL C 502

Chain	Residue
C	ARG61

---

site_id	AC7
Number of Residues	30
Details	binding site for residue FAD D 501

Chain	Residue
D	GLY54
D	VAL74
D	GLU75
D	PRO76
D	GLN83
D	PRO84
D	ARG117
D	VAL118
D	ALA144
D	LEU145
D	GLY146
D	ASN169
D	TYR170
D	CYS201
D	LYS207
D	GLY335
D	ASP336
D	LYS344
D	THR345
D	ALA346
D	ALA347
D	SER378
D	PRO380
D	LYS418
D	HOH602
D	HOH606
D	HOH626
D	HOH641
D	GLY52
D	SER53

---

site_id	AC8
Number of Residues	1
Details	binding site for residue CL D 502

Chain	Residue
D	ARG61

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"30905673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22852582","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30905673","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9R112","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9R112","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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