3HSU

Functional roles of the 6-s-cysteinyl, 8 alpha-N1-histidyl FAD in Glucooligosaccharide Oxidase from Acremonium strictum

Replaces:  3E0T

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005576	cellular_component	extracellular region
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0071949	molecular_function	FAD binding

Functional Information from PROSITE/UniProt

site_id	PS00862
Number of Residues	34
Details	OX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PaaiaiprSteDIaaaVqcgldagvq...IsakGGGH

Chain	Residue	Details
A	PRO37-HIS70

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:16154992

Chain	Residue	Details
A	TYR429

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:16154992, ECO:0007744|PDB:2AXR

Chain	Residue	Details
A	TYR72
A	THR129
A	ARG245
A	GLN353
A	GLN384
A	TYR429

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16154992, ECO:0007744|PDB:1ZR6, ECO:0007744|PDB:2AXR, ECO:0007744|PDB:3HSU

Chain	Residue	Details
A	ASN305
A	ASN341

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN394

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site_id	SWS_FT_FI5
Number of Residues	2
Details	CROSSLNK: 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys) => ECO:0000269|PubMed:16154992, ECO:0000269|PubMed:18768475

Chain	Residue	Details
A	HIS70
A	ALA130

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