3ZDN

D11-C mutant of monoamine oxidase from Aspergillus niger

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005777	cellular_component	peroxisome
A	0016491	molecular_function	oxidoreductase activity
A	0097621	molecular_function	monoamine oxidase activity
B	0005777	cellular_component	peroxisome
B	0016491	molecular_function	oxidoreductase activity
B	0097621	molecular_function	monoamine oxidase activity
C	0005777	cellular_component	peroxisome
C	0016491	molecular_function	oxidoreductase activity
C	0097621	molecular_function	monoamine oxidase activity
D	0005777	cellular_component	peroxisome
D	0016491	molecular_function	oxidoreductase activity
D	0097621	molecular_function	monoamine oxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 601

Chain	Residue
A	HIS112
A	ASN113
A	ALA114
A	LEU115
B	PHE170
B	ASP173
B	TYR176

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 601

Chain	Residue
A	TYR176
B	HIS112
B	ASN113
B	ALA114
B	LEU115
A	PHE170
A	ASP173

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 601

Chain	Residue
C	HIS112
C	ASN113
C	LEU115
C	HOH2042
D	PHE170
D	ASP173
D	TYR176

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 601

Chain	Residue
C	PHE170
C	ASP173
C	TYR176
D	HIS112
D	ASN113
D	ALA114
D	LEU115
D	HOH2023

---

site_id	AC5
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD B 1486

Chain	Residue
B	ILE45
B	GLY46
B	GLY47
B	GLY48
B	TYR49
B	CYS50
B	GLU69
B	ALA70
B	ARG71
B	GLY75
B	GLY76
B	ARG77
B	GLY91
B	GLY92
B	THR93
B	TRP94
B	PRO278
B	VAL279
B	THR307
B	PRO309
B	TRP420
B	PHE425
B	ALA429
B	GLY430
B	ASN456
B	SER457
B	SER465
B	PHE466
B	ILE467
B	ALA470
B	HOH2010
B	HOH2011
B	HOH2012
B	HOH2016
B	HOH2018
B	HOH2031
B	HOH2037
B	HOH2095
B	HOH2113

---

site_id	AC6
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD A 1487

Chain	Residue
A	HOH2018
A	HOH2020
A	HOH2033
A	HOH2043
A	HOH2117
A	HOH2139
A	ILE45
A	GLY46
A	GLY47
A	GLY48
A	TYR49
A	CYS50
A	GLU69
A	ALA70
A	ARG71
A	GLY75
A	GLY76
A	ARG77
A	GLY91
A	GLY92
A	THR93
A	TRP94
A	PRO278
A	VAL279
A	THR307
A	PRO309
A	PHE425
A	ALA429
A	ASN456
A	SER457
A	SER465
A	PHE466
A	ILE467
A	ALA470
A	HOH2010
A	HOH2012
A	HOH2017

---

site_id	AC7
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD D 1487

Chain	Residue
D	ILE45
D	GLY46
D	GLY47
D	GLY48
D	TYR49
D	CYS50
D	GLU69
D	ALA70
D	ARG71
D	GLY75
D	GLY76
D	ARG77
D	GLY91
D	GLY92
D	THR93
D	TRP94
D	VAL279
D	THR307
D	ILE308
D	PHE425
D	ALA429
D	ASN456
D	SER457
D	SER465
D	PHE466
D	ILE467
D	ALA470
D	HOH2003
D	HOH2004
D	HOH2008
D	HOH2009
D	HOH2012
D	HOH2022

---

site_id	AC8
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD C 1487

Chain	Residue
C	ILE45
C	GLY46
C	GLY48
C	TYR49
C	CYS50
C	GLU69
C	ALA70
C	ARG71
C	GLY75
C	GLY76
C	ARG77
C	GLY91
C	GLY92
C	THR93
C	TRP94
C	PRO278
C	VAL279
C	THR307
C	ILE308
C	PRO309
C	TRP420
C	PHE425
C	ALA429
C	ASN456
C	SER457
C	SER465
C	PHE466
C	ILE467
C	ALA470
C	HOH2007
C	HOH2008
C	HOH2013
C	HOH2014
C	HOH2016
C	HOH2025
C	HOH2035
C	HOH2090

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	88
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	72
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

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