3ZYX

Crystal structure of human monoamine oxidase B in complex with methylene blue and bearing the double mutation I199A-Y326A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005740	cellular_component	mitochondrial envelope
A	0005741	cellular_component	mitochondrial outer membrane
A	0008131	molecular_function	primary amine oxidase activity
A	0009055	molecular_function	electron transfer activity
A	0009410	biological_process	response to xenobiotic stimulus
A	0009636	biological_process	response to toxic substance
A	0010044	biological_process	response to aluminum ion
A	0010269	biological_process	response to selenium ion
A	0014063	biological_process	negative regulation of serotonin secretion
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0019607	biological_process	phenylethylamine catabolic process
A	0021762	biological_process	substantia nigra development
A	0030425	cellular_component	dendrite
A	0032496	biological_process	response to lipopolysaccharide
A	0042420	biological_process	dopamine catabolic process
A	0042802	molecular_function	identical protein binding
A	0043025	cellular_component	neuronal cell body
A	0045471	biological_process	response to ethanol
A	0045964	biological_process	positive regulation of dopamine metabolic process
A	0048545	biological_process	response to steroid hormone
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050665	biological_process	hydrogen peroxide biosynthetic process
A	0051412	biological_process	response to corticosterone
A	0052595	molecular_function	aliphatic amine oxidase activity
A	0097621	molecular_function	monoamine oxidase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005740	cellular_component	mitochondrial envelope
B	0005741	cellular_component	mitochondrial outer membrane
B	0008131	molecular_function	primary amine oxidase activity
B	0009055	molecular_function	electron transfer activity
B	0009410	biological_process	response to xenobiotic stimulus
B	0009636	biological_process	response to toxic substance
B	0010044	biological_process	response to aluminum ion
B	0010269	biological_process	response to selenium ion
B	0014063	biological_process	negative regulation of serotonin secretion
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0019607	biological_process	phenylethylamine catabolic process
B	0021762	biological_process	substantia nigra development
B	0030425	cellular_component	dendrite
B	0032496	biological_process	response to lipopolysaccharide
B	0042420	biological_process	dopamine catabolic process
B	0042802	molecular_function	identical protein binding
B	0043025	cellular_component	neuronal cell body
B	0045471	biological_process	response to ethanol
B	0045964	biological_process	positive regulation of dopamine metabolic process
B	0048545	biological_process	response to steroid hormone
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050665	biological_process	hydrogen peroxide biosynthetic process
B	0051412	biological_process	response to corticosterone
B	0052595	molecular_function	aliphatic amine oxidase activity
B	0097621	molecular_function	monoamine oxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD A 600

Chain	Residue
A	GLY11
A	GLY41
A	ARG42
A	THR43
A	GLY58
A	SER59
A	TYR60
A	ARG233
A	PRO234
A	VAL235
A	ALA263
A	GLY13
A	ILE264
A	TRP388
A	TYR393
A	CYS397
A	TYR398
A	GLY425
A	THR426
A	GLY434
A	TYR435
A	MET436
A	ILE14
A	ALA439
A	MBT601
A	HOH2001
A	HOH2002
A	HOH2007
A	HOH2009
A	HOH2014
A	HOH2030
A	HOH2035
A	HOH2110
A	SER15
A	LEU33
A	GLU34
A	ALA35
A	ARG36
A	GLY40

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE MBT A 601

Chain	Residue
A	LEU171
A	ALA199
A	GLN206
A	THR314
A	ILE316
A	THR327
A	LEU328
A	PHE343
A	TYR398
A	TYR435
A	FAD600
A	HOH2103
A	HOH2166

---

site_id	AC3
Number of Residues	40
Details	BINDING SITE FOR RESIDUE FAD B 600

Chain	Residue
B	VAL10
B	GLY11
B	GLY13
B	ILE14
B	SER15
B	LEU33
B	GLU34
B	ALA35
B	ARG36
B	GLY40
B	GLY41
B	ARG42
B	THR43
B	GLY58
B	SER59
B	TYR60
B	ARG233
B	PRO234
B	VAL235
B	ALA263
B	ILE264
B	TRP388
B	TYR393
B	CYS397
B	TYR398
B	GLY425
B	THR426
B	GLY434
B	TYR435
B	MET436
B	ALA439
B	MBT601
B	HOH2001
B	HOH2002
B	HOH2009
B	HOH2012
B	HOH2015
B	HOH2032
B	HOH2039
B	HOH2117

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MBT B 601

Chain	Residue
B	FAD600
B	HOH2107
B	HOH2162
B	LEU171
B	ALA199
B	GLN206
B	THR314
B	ILE316
B	LEU328
B	PHE343

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	974
Details	TOPO_DOM: Cytoplasmic

Chain	Residue	Details
A	SER2-VAL489
B	SER2-VAL489

---

site_id	SWS_FT_FI2
Number of Residues	52
Details	TRANSMEM: Helical; Anchor for type IV membrane protein

Chain	Residue	Details
A	PRO490-LEU516
B	PRO490-LEU516

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	TOPO_DOM: Mitochondrial intermembrane

Chain	Residue	Details
A	LEU517-VAL520
B	LEU517-VAL520

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Important for catalytic activity

Chain	Residue	Details
A	CYS156
A	CYS365
A	HIS382
B	CYS156
B	CYS365
B	HIS382

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:11049757

Chain	Residue	Details
A	SER2
B	SER2

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BW75

Chain	Residue	Details
A	LYS52
B	LYS52

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: S-8alpha-FAD cysteine => ECO:0000269|PubMed:11753429, ECO:0000269|PubMed:12913124, ECO:0000269|PubMed:15027868, ECO:0000269|PubMed:15710600, ECO:0000269|PubMed:16366596, ECO:0007744|PDB:1GOS, ECO:0007744|PDB:1OJ9, ECO:0007744|PDB:1OJA, ECO:0007744|PDB:1OJC, ECO:0007744|PDB:1OJD, ECO:0007744|PDB:1S2Q, ECO:0007744|PDB:1S2Y, ECO:0007744|PDB:1S3B, ECO:0007744|PDB:1S3E, ECO:0007744|PDB:2BK3, ECO:0007744|PDB:2BK4, ECO:0007744|PDB:2BK5, ECO:0007744|PDB:2BYB, ECO:0007744|PDB:2C64, ECO:0007744|PDB:2C65, ECO:0007744|PDB:2C66, ECO:0007744|PDB:2C67, ECO:0007744|PDB:2C70, ECO:0007744|PDB:2C72, ECO:0007744|PDB:2C73, ECO:0007744|PDB:2C75, ECO:0007744|PDB:2C76, ECO:0007744|PDB:2V5Z, ECO:0007744|PDB:2V60, ECO:0007744|PDB:2V61, ECO:0007744|PDB:2VRL, ECO:0007744|PDB:2VRM, ECO:0007744|PDB:2VZ2, ECO:0007744|PDB:2XFN, ECO:0007744|PDB:2XFO, ECO:0007744|PDB:2XFP, ECO:0007744|PDB:2XFQ, ECO:0007744|PDB:3PO7, ECO:0007744|PDB:3ZYX, ECO:0007744|PDB:4A79, ECO:0007744|PDB:4A7A, ECO:0007744|PDB:4CRT, ECO:0007744|PDB:5MRL

Chain	Residue	Details
A	CYS397
B	CYS397

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