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1EOI

CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE COMPLEXED WITH THE TRANSITION STATE ANALOG MOLYBDATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003993molecular_functionacid phosphatase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
B0003993molecular_functionacid phosphatase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
C0003993molecular_functionacid phosphatase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MOO A 1001
ChainResidue
ALYS115
AARG122
ALEU140
ASER148
AGLY149
AHIS150
AARG183
AHIS189

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MOO B 1002
ChainResidue
BARG122
BLEU140
BSER148
BGLY149
BHIS150
BARG183
BHIS189
BLYS115

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MOO C 1003
ChainResidue
CLYS115
CARG122
CLEU140
CSER148
CGLY149
CHIS150
CARG183
CHIS189

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
DetailsAnnotated By Reference To The Literature 1d2t
ChainResidueDetails
AHIS189
AASP193
AARG183
AHIS150

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d2t
ChainResidueDetails
BHIS189
BASP193
BARG183
BHIS150

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d2t
ChainResidueDetails
CHIS189
CASP193
CARG183
CHIS150

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PDB entries from 2024-08-21

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