1SKB

Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic dynamics

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003993	molecular_function	acid phosphatase activity
A	0005576	cellular_component	extracellular region
A	0016158	molecular_function	inositol hexakisphosphate 3-phosphatase activity
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity

Functional Information from PROSITE/UniProt

site_id	PS00616
Number of Residues	15
Details	HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. ItlVqvLsRHGaRyP

Chain	Residue	Details
A	ILE50-PRO64

site_id	PS00778
Number of Residues	17
Details	HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. MyVDfSHDNSMvsIffA

Chain	Residue	Details
A	MET332-ALA348

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15136045","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QWO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15341723","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1SK8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15341723","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1SK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SK9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P34752","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15136045","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15341723","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QWO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SKB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15136045","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15341723","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QWO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SK9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SKA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SKB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15136045","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QWO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1rpt