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2YY6

Crystal Structure of the phosphoglycolate phosphatase from Aquifex aeolicus VF5

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006281biological_processDNA repair
A0008967molecular_functionphosphoglycolate phosphatase activity
A0016787molecular_functionhydrolase activity
A0046295biological_processglycolate biosynthetic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006281biological_processDNA repair
B0008967molecular_functionphosphoglycolate phosphatase activity
B0016787molecular_functionhydrolase activity
B0046295biological_processglycolate biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
APRO37
AASP38
AASN39
ALYS42
ATYR43

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BPRO37
BASP38
BASN39
BTYR43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
ASER104
ALYS137

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
BSER104
BLYS137

243083

PDB entries from 2025-10-15

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