Structure of PDB 2v5z Chain A

Receptor sequence

>2v5zA (length=499) Species: 9606 (Homo sapiens) [Search protein sequence]

NKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVK
YVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGP
FPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELL
DKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTT
NGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNH
EMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYK
EPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKL
ARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYF
PPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILH
AMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTI

3D structure

PDB

2v5z Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs.

Chain

Resolution

1.6 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	G62 R197 K296
Catalytic site (residue number reindexed from 1)	G60 R195 K294
Enzyme Commision number	1.4.3.21: primary-amine oxidase. 1.4.3.4: monoamine oxidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FAD	A	G11 G13 S15 L33 E34 A35 R36 G41 R42 G57 G58 S59 Y60 P234 V235 I264 W388 Y393 C397 Y398 G425 T426 G434 Y435 M436	G9 G11 S13 L31 E32 A33 R34 G39 R40 G55 G56 S57 Y58 P232 V233 I262 W386 Y391 C395 Y396 G423 T424 G432 Y433 M434
BS02	SAG	A	L171 C172 I199 Q206 I316 Y326 Y435	L169 C170 I197 Q204 I314 Y324 Y433	MOAD: Ki=0.45uM

Gene Ontology

	Molecular Function
GO:0005515	protein binding
GO:0008131	primary methylamine oxidase activity
GO:0009055	electron transfer activity
GO:0016491	oxidoreductase activity
GO:0042802	identical protein binding
GO:0050660	flavin adenine dinucleotide binding
GO:0052595	aliphatic amine oxidase activity
GO:0097621	monoamine oxidase activity

	Biological Process
GO:0009410	response to xenobiotic stimulus
GO:0009636	response to toxic substance
GO:0010044	response to aluminum ion
GO:0010269	response to selenium ion
GO:0014063	negative regulation of serotonin secretion
GO:0019607	phenylethylamine catabolic process
GO:0021762	substantia nigra development
GO:0032496	response to lipopolysaccharide
GO:0042420	dopamine catabolic process
GO:0045471	response to ethanol
GO:0045964	positive regulation of dopamine metabolic process
GO:0048545	response to steroid hormone
GO:0050665	hydrogen peroxide biosynthetic process
GO:0051412	response to corticosterone

	Cellular Component
GO:0005739	mitochondrion
GO:0005740	mitochondrial envelope
GO:0005741	mitochondrial outer membrane
GO:0030425	dendrite
GO:0043025	neuronal cell body

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:2v5z, PDBe:2v5z, PDBj:2v5z
PDBsum	2v5z
PubMed	17915852
UniProt	P27338\|AOFB_HUMAN Amine oxidase [flavin-containing] B (Gene Name=MAOB)

[Back to BioLiP]