Structure of PDB 1lvn Chain A

Receptor sequence
>1lvnA (length=718) Species: 562 (Escherichia coli) [Search protein sequence]
MVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLA
LQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQ
AVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIM
LDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFA
AAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNY
WAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPM
QIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKV
MYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSNA
VLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELV
VRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAK
DDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAG
GPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQII
PYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPN
RSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHT
LLKPWNFFDETPTLGALK
3D structure
PDB1lvn Medical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y369 D383 H524 H526 H689
Catalytic site (residue number reindexed from 1) Y363 D377 H517 H519 H682
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 A H524 H526 H689 H518 H520 H683
BS02 CA A D533 L534 D535 D678 A679 D527 L528 D529 D672 A673
BS03 CA A E573 H644 Y667 E672 E567 H638 Y661 E666
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0005509 calcium 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
Biological Process
GO:0006559 L-phenylalanine catabolic process
GO:0009308 amine metabolic process
GO:0019607 phenylethylamine catabolic process
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lvn, PDBe:1lvn, PDBj:1lvn
PDBsum1lvn
PubMed15498552
UniProtP46883|AMO_ECOLI Primary amine oxidase (Gene Name=tynA)

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