Structure of PDB 1w2z Chain C

Receptor sequence
>1w2zC (length=642) Species: 3888 (Pisum sativum) [Search protein sequence]
VQHPLDPLTKEEFLAVQTIVQNKYPISNNRLAFHYIGLDDPEKDHVLRYE
THPTLVSIPRKIFVVAIINSQTHEILINLRIRSIVSDNIHNGYGFPILSV
DEQSLAIKLPLKYPPFIDSVKKRGLNLSEIVCSSFTMGWFGEEKNVRTVR
LDCFMKESTVNIYVRPITGITIVADLDLMKIVEYHDRDIEAVPTAENTEY
QVSKQSPPFGPKQHSLTSHQPQGPGFQINGHSVSWANWKFHIGFDVRAGI
VISLASIYDLEKHKSRRVLYKGYISELFVPYQDPTEEFYFKTFFDSGEFG
FGLSTVSLIPNRDCPPHAQFIDTYVHSANGTPILLKNAICVFEQYGNIMW
RHTENGIPNESIEESRTEVNLIVRTIVTVGNYDNVIDWEFKASGSIKPSI
ALSGILEIKGTNIKHKDEIKEDLHGKLVSANSIGIYHDHFYIYYLDFDID
GTHNSFEKTSLKTVRIKDGSSKRKSYWTTETQTAKTESDAKITIGLAPAE
LVVVNPNIKTAVGNEVGYRLIPAIPAHPLLTEDDYPQIRGAFTNYNVWVT
AYNRTEKWAGGLYVDHSRGDDTLAVWTKQNREIVNKDIVMWHVVGIHHVP
AQEDFPIMPLLSTSFELRPTNFFERNPVLKTLSPRDVAWPGC
3D structure
PDB1w2z Using Xenon as a Probe for Dioxygen-Binding Sites in Copper Amine Oxidases.
ChainC
Resolution2.24 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) Y286 D300 Y387 H442 H444 H603
Catalytic site (residue number reindexed from 1) Y281 D295 Y382 H437 H439 H598
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 C H442 H444 H603 H437 H439 H598
BS02 MN C D451 F452 D453 D592 I593 D446 F447 D448 D587 I588
BS03 XE C F452 Y523 R524 L525 M595 F447 Y518 R519 L520 M590
BS04 XE C L407 Y446 T618 L402 Y441 T613
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0008131 primary methylamine oxidase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0048038 quinone binding
GO:0052595 aliphatic amine oxidase activity
GO:0052597 diamine oxidase activity
Biological Process
GO:0009308 amine metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1w2z, PDBe:1w2z, PDBj:1w2z
PDBsum1w2z
PubMed15533431
UniProtQ43077|AMO_PEA Primary amine oxidase

[Back to BioLiP]