Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4CRT

Crystal structure of human monoamine oxidase B in complex with the multi-target inhibitor ASS234

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	44
Details	Binding site for residues FAD A 600 and ASS A 601

Chain	Residue
A	VAL10
A	GLY40
A	GLY41
A	ARG42
A	THR43
A	GLY58
A	SER59
A	TYR60
A	LEU171
A	CYS172
A	ILE199
A	GLY11
A	GLN206
A	PRO234
A	VAL235
A	ALA263
A	ILE264
A	TYR326
A	PHE343
A	TRP388
A	TYR393
A	CYS397
A	GLY13
A	TYR398
A	GLY425
A	THR426
A	GLY434
A	TYR435
A	MET436
A	ALA439
A	HOH2001
A	HOH2002
A	HOH2012
A	ILE14
A	HOH2015
A	HOH2021
A	HOH2048
A	HOH2055
A	HOH2187
A	SER15
A	LEU33
A	GLU34
A	ALA35
A	ARG36

site_id	AC2
Number of Residues	43
Details	Binding site for residues FAD B 600 and ASS B 601

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	LEU171
B	ILE199
B	GLN206
B	PRO234
B	VAL235
B	ALA263
B	ILE264
B	TYR326
B	PHE343
B	TRP388
B	TYR393
B	CYS397
B	TYR398
B	GLY425
B	THR426
B	GLY434
B	TYR435
B	MET436
B	ALA439
B	HOH2002
B	HOH2003
B	HOH2021
B	HOH2026
B	HOH2035
B	HOH2064
B	HOH2073
B	HOH2221

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)