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1RKQ

Crystal structure of HAD-like phosphatase yidA from E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005829cellular_componentcytosol
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0046872molecular_functionmetal ion binding
A0050308molecular_functionsugar-phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0005829cellular_componentcytosol
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0046872molecular_functionmetal ion binding
B0050308molecular_functionsugar-phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 1272
ChainResidue
AASP10
AGLY45
ALYS198
AASN224
AHOH1276

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 2272
ChainResidue
BHOH2276
BASP10
BGLY45
BLYS198
BASN224

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1273
ChainResidue
AASP10
AASP12
AASP221
AHOH1274
AHOH1275
AHOH1276

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 2273
ChainResidue
BASP10
BASP12
BASP221
BHOH2274
BHOH2275
BHOH2276

Functional Information from PROSITE/UniProt
site_idPS01228
Number of Residues12
DetailsCOF_1 Hypothetical cof family signature 1. LIaiDMDGTLLL
ChainResidueDetails
ALEU6-LEU17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:16990279
ChainResidueDetails
AASP10
BASP10

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP10
AASP12
AASP221
BASP10
BASP12
BASP221

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AMET11
ATHR44
ALYS198
AASN224
BMET11
BTHR44
BLYS198
BASN224

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PDB entries from 2024-07-17

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