Structure of PDB 1n9e Chain D

Receptor sequence
>1n9eD (length=735) Species: 4922 (Komagataella pastoris) [Search protein sequence]
ASAECVSNENVEIEAPKTNIWTSLAKEEVQEVLDLLHSTYNITEVTKADF
FSNYVLWIETLKPNKTEALTYLDEDGDLPPRNARTVVYFGEGEEGYFEEL
KVGPLPVSDETTIEPLSFYNTNGKSKLPFEVGHLDRIKSAAKSSFLNKNL
NTTIMRDVLEGLIGVPYEDMGCHSAAPQLHDPATGATVDYGTCNINTEND
AENLVPTGFFFKFDMTGRDVSQWKMLEYIYNNKVYTSAEELYEAMQKDDF
VTLPKIDVDNLDWTVIQRNDSAPIRHLDDRKSPRLVEPEGRRWAYDGEEE
YFSWMDWGFYTSWSRDTGISFYDITFKGERIVYELSLQELIAEYGSDDPF
NQHTFYSDISYGVGNRFSLVPGYDCPATAGYFTTDTFEYDEFYNRTLSYC
VFENQEDYSLLRHTGASYSAITQNPTLNVRFISTIGNYDYNFLYKFFLDG
TLEVSVRAAGYIQAGYWNPETSAPYGLKIHDVLSGSFHDHVLNYKVDLDV
GGTKNRASKYVMKDVDVEYPWAPGTVYNTKQIAREVLEKEDFNGINWPEN
GQGILLIESAEETNSFGNPRAYNIMPGGGGVHRIVKNSRSGPETQNWARS
NLFLTKHKDEELRSSTALNTNALYDPPVNFNAFLDDESLDGEDIVAWVNL
GLHHLPNSNDLPNTIFSTAHASFMLTPFNYFDSENSRDTTQQVFYTYDDE
TEESNWEFYGNDWSSCGLEVPEPNFEDYTYGRGTR
3D structure
PDB1n9e The Crystal Structure of Pichia pastoris Lysyl Oxidase
ChainD
Resolution1.65 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) Y384 D398 Y478 H528 H530 H694
Catalytic site (residue number reindexed from 1) Y344 D358 Y438 H488 H490 H654
Enzyme Commision number 1.4.3.-
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 D A478 H528 H530 H694 A438 H488 H490 H654
BS02 CA D D537 L538 D539 D683 I684 D497 L498 D499 D643 I644
BS03 CA D E580 F673 D675 E677 E540 F633 D635 E637
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0008131 primary methylamine oxidase activity
GO:0048038 quinone binding
Biological Process
GO:0009308 amine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1n9e, PDBe:1n9e, PDBj:1n9e
PDBsum1n9e
PubMed14690425
UniProtQ96X16

[Back to BioLiP]