1CC8

CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006825	biological_process	copper ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0016531	molecular_function	copper chaperone activity
A	0034599	biological_process	cellular response to oxidative stress
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 74

Chain	Residue
A	THR14
A	CYS15
A	CYS18

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BEN A 186

Chain	Residue
A	LEU73
A	HOH1002
A	ILE4
A	ASN23
A	GLU30
A	VAL33
A	SER34
A	ILE36

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site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BEN A 187

Chain	Residue
A	MET13
A	LEU40
A	GLN43
A	GLU58
A	HOH1039
A	HOH1100
A	HOH1109

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Functional Information from PROSITE/UniProt

site_id	PS01047
Number of Residues	31
Details	HMA_1 Heavy-metal-associated domain. NvVMtCsGCsgaVNkvLtklepdvskidIsL

Chain	Residue	Details
A	ASN10-LEU40

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280, ECO:0000269|PubMed:11327811, ECO:0000269|PubMed:19965379, ECO:0000269|PubMed:28865724, ECO:0007744|PDB:1FD8, ECO:0007744|PDB:3K7R, ECO:0007744|PDB:5VDE, ECO:0007744|PDB:5VDF

Chain	Residue	Details
A	CYS15
A	CYS18

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