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1QFX

PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

Functional Information from GO Data
ChainGOidnamespacecontents
A0003993molecular_functionacid phosphatase activity
A0009277cellular_componentfungal-type cell wall
A0016158molecular_function3-phytase activity
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
B0003993molecular_functionacid phosphatase activity
B0009277cellular_componentfungal-type cell wall
B0016158molecular_function3-phytase activity
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
Functional Information from PROSITE/UniProt
site_idPS00616
Number of Residues15
DetailsHIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. VdqVimVkRHGeRyP
ChainResidueDetails
AVAL54-PRO68

site_idPS00778
Number of Residues17
DetailsHIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. LfFNfAHDTNItpIlaA
ChainResidueDetails
ALEU312-ALA328

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AHIS63
BHIS63

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AASP319
BASP319

site_idSWS_FT_FI3
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN172
AASN296
AASN439
BASN172
BASN296
BASN439

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1rpt
ChainResidueDetails
AARG156
AASP319
AARG62
AHIS318
AARG66
AHIS63

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1rpt
ChainResidueDetails
BARG156
BASP319
BARG62
BHIS318
BARG66
BHIS63

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PDB entries from 2024-07-31

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