Structure of PDB 3hii Chain A

Receptor sequence
>3hiiA (length=715) Species: 9606 (Homo sapiens) [Search protein sequence]
PRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSSTTTMAKNTVFLIEMLL
PKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLPGPCYMR
ALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQD
CHDRCLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGST
DAGHWAVEQVWYNGKFYGSPEELARKYADGEVDVVVLEDPLEPPLFSSHK
PRGDFPSPIHVSGPRLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQV
LNVHFGGERIAYEVSVQEAVALYGGHTPAGMQTKYLDVGWGLGSVTHELA
PGIDCPETATFLDTFHYYDADDPVHYPRALCLFEMPTGVPLRRHFNSNFK
GGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMHATGYVH
ATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKL
ENITNPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENP
WGHKRSYRLQIHSMADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSS
IYHQNDPWDPPVVFEQFLHNNENIENEDLVAWVTVGFLHIPHSEDIPNTA
TPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRDNGPNYVQRWIPEDRDC
SMPPPFSYNGTYRPV
3D structure
PDB3hii Structure and inhibition of human diamine oxidase
ChainA
Resolution2.149 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y359 D373 Y461 H510 H512 H675
Catalytic site (residue number reindexed from 1) Y323 D337 Y425 H474 H476 H639
Enzyme Commision number 1.4.3.22: diamine 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 A A461 H510 H512 H675 A425 H474 H476 H639
BS02 CA A D519 L520 D521 D664 L665 D483 L484 D485 D628 L629
BS03 CA A E562 F653 N656 E658 E526 F617 N620 E622
BS04 PNT A Y148 Y371 D373 W376 V381 Y404 V458 Y459 N460 Y122 Y335 D337 W340 V345 Y368 V422 Y423 N424 MOAD: Ki=290nM
PDBbind-CN: -logKd/Ki=6.54,Ki=290nM
BindingDB: Ki=290nM
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:0008201 heparin binding
GO:0016491 oxidoreductase activity
GO:0016641 oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0048038 quinone binding
GO:0050232 putrescine oxidase activity
GO:0052597 diamine oxidase activity
GO:0052598 histamine oxidase activity
Biological Process
GO:0009308 amine metabolic process
GO:0009445 putrescine metabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005777 peroxisome
GO:0005886 plasma membrane
GO:0005923 bicellular tight junction
GO:0035580 specific granule lumen
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3hii, PDBe:3hii, PDBj:3hii
PDBsum3hii
PubMed19764817
UniProtP19801|AOC1_HUMAN Diamine oxidase [copper-containing] (Gene Name=AOC1)

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