Structure of PDB 1pu4 Chain B

Receptor sequence
>1pu4B (length=699) Species: 9606 (Homo sapiens) [Search protein sequence]
SQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPK
AAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVT
VERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKRGRN
LVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPA
RWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVP
PGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGE
RLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYL
ATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAE
TVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGATGKY
GNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPEH
QLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQM
LSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPT
VDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRP
YNFFDEDPSFYSADSIYFRGDQDAGACEVNPLACACAPDLPAFSHGGFS
3D structure
PDB1pu4 Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.
ChainB
Resolution3.2 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) Y372 D386 Y471 H520 H522 H684
Catalytic site (residue number reindexed from 1) Y315 D329 Y414 H463 H465 H627
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 A471 H520 H522 H684 A414 H463 H465 H627
BS02 CA B D529 L530 D531 D673 L674 D472 L473 D474 D616 L617
BS03 CA B E572 K638 E641 F663 N665 E667 E515 K581 E584 F606 N608 E610
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1pu4, PDBe:1pu4, PDBj:1pu4
PDBsum1pu4
PubMed16046623
UniProtQ16853|AOC3_HUMAN Amine oxidase [copper-containing] 3 (Gene Name=AOC3)

[Back to BioLiP]