Structure of PDB 4bty Chain B

Receptor sequence
>4btyB (length=707) Species: 9606 (Homo sapiens) [Search protein sequence]
SQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPK
AAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVT
VERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKHRGR
NLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDP
ARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPV
PPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQG
ERLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPY
LATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLA
ETVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGATGK
YGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPE
HQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQ
MLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAP
TVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLR
PYNFFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFS
HGGFSHN
3D structure
PDB4bty Novel Pyridazinone Inhibitors for Vascular Adhesion Protein- 1 (Vap-1): Old Target - New Inhibition Mode.
ChainB
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y372 D386 Y471 H520 H522 H684
Catalytic site (residue number reindexed from 1) Y316 D330 Y415 H464 H466 H628
Enzyme Commision number 1.4.3.21: primary-amine 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 CU B H520 H522 H684 H464 H466 H628
BS02 CA B D529 L530 D531 D673 L674 D473 L474 D475 D617 L618
BS03 CA B E572 E641 F663 N665 E667 E516 E585 F607 N609 E611
BS04 JWF B F173 Y176 L177 D180 T210 T212 F389 Y394 L469 H762 F117 Y120 L121 D124 T154 T156 F333 Y338 L413 H706 PDBbind-CN: -logKd/Ki=7.70,IC50=0.020uM
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008131 primary methylamine oxidase activity
GO:0016491 oxidoreductase activity
GO:0016641 oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0046982 protein heterodimerization activity
GO:0048038 quinone binding
GO:0052595 aliphatic amine oxidase activity
Biological Process
GO:0006954 inflammatory response
GO:0007155 cell adhesion
GO:0009308 amine metabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005737 cytoplasm
GO:0005769 early endosome
GO:0005783 endoplasmic reticulum
GO:0005794 Golgi apparatus
GO:0005886 plasma membrane
GO:0005902 microvillus
GO:0009986 cell surface
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4bty, PDBe:4bty, PDBj:4bty
PDBsum4bty
PubMed24304424
UniProtQ16853|AOC3_HUMAN Amine oxidase [copper-containing] 3 (Gene Name=AOC3)

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