1S3E

Crystal structure of MAOB in complex with 6-hydroxy-N-propargyl-1(R)-aminoindan

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	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	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	38
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	PRO234
A	VAL235
A	ALA263
A	ILE264
A	GLY13
A	TRP388
A	TYR393
A	CYS397
A	TYR398
A	GLY425
A	THR426
A	GLY434
A	TYR435
A	MET436
A	ALA439
A	ILE14
A	RHP601
A	HOH607
A	HOH609
A	HOH614
A	HOH615
A	HOH616
A	HOH622
A	HOH654
A	HOH693
A	SER15
A	LEU33
A	GLU34
A	ALA35
A	ARG36
A	GLY40

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE RHP A 601

Chain	Residue
A	LEU171
A	CYS172
A	ILE198
A	GLN206
A	TYR326
A	TYR398
A	TYR435
A	FAD600

---

site_id	AC3
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD B 600

Chain	Residue
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	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	RHP601
B	HOH604
B	HOH607
B	HOH615
B	HOH628
B	HOH629
B	HOH631
B	HOH644
B	HOH649

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE RHP B 601

Chain	Residue
B	LEU171
B	CYS172
B	ILE198
B	GLN206
B	TYR326
B	TYR398
B	TYR435
B	FAD600

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	974
Details	TOPO_DOM: Cytoplasmic

Chain	Residue	Details
A	ASN3-PRO490
B	ASN3-PRO490

---

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

Chain	Residue	Details
A	GLY491-LEU517
B	GLY491-LEU517

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Important for catalytic activity

Chain	Residue	Details
A	TYR383
B	TRP157
B	GLU366
B	TYR383
A	TRP157
A	GLU366

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:11049757

Chain	Residue	Details
A	ASN3
B	ASN3

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BW75

Chain	Residue	Details
A	TYR53
B	TYR53

---

site_id	SWS_FT_FI6
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	TYR398
B	TYR398

---