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2BQ8

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

Functional Information from GO Data
ChainGOidnamespacecontents
X0003993molecular_functionacid phosphatase activity
X0005764cellular_componentlysosome
X0005829cellular_componentcytosol
X0006809biological_processnitric oxide biosynthetic process
X0008198molecular_functionferrous iron binding
X0008199molecular_functionferric iron binding
X0010936biological_processnegative regulation of macrophage cytokine production
X0016020cellular_componentmembrane
X0016311biological_processdephosphorylation
X0016787molecular_functionhydrolase activity
X0032496biological_processresponse to lipopolysaccharide
X0032691biological_processnegative regulation of interleukin-1 beta production
X0032695biological_processnegative regulation of interleukin-12 production
X0032720biological_processnegative regulation of tumor necrosis factor production
X0032929biological_processnegative regulation of superoxide anion generation
X0034097biological_processresponse to cytokine
X0042554biological_processsuperoxide anion generation
X0045019biological_processnegative regulation of nitric oxide biosynthetic process
X0045453biological_processbone resorption
X0046872molecular_functionmetal ion binding
X0050728biological_processnegative regulation of inflammatory response
X0050830biological_processdefense response to Gram-positive bacterium
X0060349biological_processbone morphogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE2 X1305
ChainResidue
XASP12
XASP50
XTYR53
XASP145
XHIS221
XFE21306
XHOH2080

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE2 X1306
ChainResidue
XHIS184
XHIS219
XFE21305
XHOH2080
XHOH2110
XASP50
XASP145

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN X1307
ChainResidue
XHIS22
XGLU67
XASP71

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 X1308
ChainResidue
XARG79
XSER106
XLYS107
XARG108
XHOH2147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING:
ChainResidueDetails
XASP12
XASN89
XHIS184
XHIS219
XHIS221
XASP50
XTYR53

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15993892
ChainResidueDetails
XASN95

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
XASN126

218500

PDB entries from 2024-04-17

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