5ZE3

Crystal structure of human lysyl oxidase-like 2 (hLOXL2) in a precursor state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0016020	cellular_component	membrane
A	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
B	0005507	molecular_function	copper ion binding
B	0016020	cellular_component	membrane
B	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor

Functional Information from PROSITE/UniProt

site_id	PS00420
Number of Residues	38
Details	SRCR_1 SRCR domain signature. GayigeGrvEvlkngeWGtvCddkWdlvsasvvCrelG

Chain	Residue	Details
A	GLY331-GLY368

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site_id	PS00926
Number of Residues	14
Details	LYSYL_OXIDASE Lysyl oxidase putative copper-binding region signature. WiWHdCHrHYHSME

Chain	Residue	Details
A	TRP620-GLU633

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000305|PubMed:29581294

Chain	Residue	Details
A	ASP549
B	ASP549
B	LEU550
B	HIS626
B	HIS628
B	HIS630
B	GLU722
B	ASP724
B	ASN727
B	ASN728
A	LEU550
A	HIS626
A	HIS628
A	HIS630
A	GLU722
A	ASP724
A	ASN727
A	ASN728

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:29581294

Chain	Residue	Details
A	TYR689
B	TYR689

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:23319596

Chain	Residue	Details
A	GLN455
B	GLN455

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:23319596, ECO:0000269|PubMed:29581294, ECO:0007744|PDB:5ZE3

Chain	Residue	Details
A	ASN644
B	ASN644

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site_id	SWS_FT_FI5
Number of Residues	4
Details	CROSSLNK: Lysine tyrosylquinone (Lys-Tyr) => ECO:0000269|PubMed:23319596, ECO:0000269|PubMed:29581294

Chain	Residue	Details
A	LYS653
A	TYR689
B	LYS653
B	TYR689

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