7B0Z

Crystal Structure of human monoamine oxidase B in complex with (E)-3-phenyl-1-(4-(trifluoromethyl)phenyl)prop-2-en-1-one

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 methylamine oxidase activity
A	0009055	molecular_function	electron transfer activity
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0021762	biological_process	substantia nigra development
A	0042420	biological_process	dopamine catabolic process
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050665	biological_process	hydrogen peroxide biosynthetic process
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 methylamine oxidase activity
B	0009055	molecular_function	electron transfer activity
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0021762	biological_process	substantia nigra development
B	0042420	biological_process	dopamine catabolic process
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050665	biological_process	hydrogen peroxide biosynthetic process
B	0097621	molecular_function	monoamine oxidase activity

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

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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

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site_id	SWS_FT_FI3
Number of Residues	6
Details	TOPO_DOM: Mitochondrial intermembrane

Chain	Residue	Details
A	LEU517-VAL520
B	LEU517-VAL520

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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

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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

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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

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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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