7NUT

Crystal structure of human AMDHD2 in complex with Zn and GlcN6P

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005829	cellular_component	cytosol
A	0006040	biological_process	amino sugar metabolic process
A	0006044	biological_process	N-acetylglucosamine metabolic process
A	0006046	biological_process	N-acetylglucosamine catabolic process
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0008448	molecular_function	N-acetylglucosamine-6-phosphate deacetylase activity
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0019262	biological_process	N-acetylneuraminate catabolic process
A	0046872	molecular_function	metal ion binding
A	0047419	molecular_function	N-acetylgalactosamine-6-phosphate deacetylase activity
A	0106279	biological_process	negative regulation of UDP-N-acetylglucosamine biosynthetic process
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005829	cellular_component	cytosol
B	0006040	biological_process	amino sugar metabolic process
B	0006044	biological_process	N-acetylglucosamine metabolic process
B	0006046	biological_process	N-acetylglucosamine catabolic process
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0008448	molecular_function	N-acetylglucosamine-6-phosphate deacetylase activity
B	0016787	molecular_function	hydrolase activity
B	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B	0019262	biological_process	N-acetylneuraminate catabolic process
B	0046872	molecular_function	metal ion binding
B	0047419	molecular_function	N-acetylgalactosamine-6-phosphate deacetylase activity
B	0106279	biological_process	negative regulation of UDP-N-acetylglucosamine biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00501
Number of Residues	8
Details	SPASE_I_1 Signal peptidases I serine active site. GCSMESAL

Chain	Residue	Details
A	GLY347-LEU354

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P0AF18

Chain	Residue	Details
A	ASP294
B	ASP294

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site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P0AF18

Chain	Residue	Details
A	GLU143
B	ALA154
B	HIS211
B	HIS232
B	ASN235
B	ARG243
B	ASP269
B	LEU328
A	ALA154
A	HIS211
A	HIS232
A	ASN235
A	ARG243
A	ASP269
A	LEU328
B	GLU143

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