2BQ8

Crystal structure of human purple acid phosphatase with an inhibitory conformation of the repression loop

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0003993	molecular_function	acid phosphatase activity
X	0005764	cellular_component	lysosome
X	0005829	cellular_component	cytosol
X	0008198	molecular_function	ferrous iron binding
X	0008199	molecular_function	ferric iron binding
X	0016020	cellular_component	membrane
X	0016787	molecular_function	hydrolase activity
X	0045453	biological_process	bone resorption
X	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FE2 X1305

Chain	Residue
X	ASP12
X	ASP50
X	TYR53
X	ASP145
X	HIS221
X	FE21306
X	HOH2080

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FE2 X1306

Chain	Residue
X	HIS184
X	HIS219
X	FE21305
X	HOH2080
X	HOH2110
X	ASP50
X	ASP145

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN X1307

Chain	Residue
X	HIS22
X	GLU67
X	ASP71

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 X1308

Chain	Residue
X	ARG79
X	SER106
X	LYS107
X	ARG108
X	HOH2147

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15993892","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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