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1D2T

CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003993molecular_functionacid phosphatase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 232
ChainResidue
ALYS115
AARG122
ASER148
AGLY149
AHIS150
AHIS189
AHOH259

Functional Information from PROSITE/UniProt
site_idPS01157
Number of Residues8
DetailsACID_PHOSPH_CL_A Class A bacterial acid phosphatases signature. GSYPSGHT
ChainResidueDetails
AGLY144-THR151

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10835340, 9260289
ChainResidueDetails
AHIS189
AASP193
AARG183
AHIS150

site_idMCSA1
Number of Residues4
DetailsM-CSA 558
ChainResidueDetails
AHIS150proton shuttle (general acid/base)
AARG183electrostatic stabiliser
AHIS189covalent catalysis
AASP193enhance reactivity

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PDB entries from 2025-07-30

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