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1YDY

Crystal structure of periplasmic glycerophosphodiester phosphodiesterase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0006629biological_processlipid metabolic process
A0008081molecular_functionphosphoric diester hydrolase activity
B0006629biological_processlipid metabolic process
B0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 903
ChainResidue
BGLU63
BASP65
BGLU171
BGOL901
BHOH906
BHOH1052

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 904
ChainResidue
AGOL902
AHOH905
AHOH1043
AGLU63
AASP65
AGLU171

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 901
ChainResidue
BHIS36
BGLU63
BGLU171
BGLN208
BPHE210
BLEU235
BTYR313
BCA903
BHOH906
BHOH1104

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 902
ChainResidue
AHIS36
AGLU63
AGLU171
AGLN208
APHE210
ALEU235
ATYR313
ACA904
AHOH905
AHOH1098
AHOH1185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q8RB32
ChainResidueDetails
AHIS36
BHIS36

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q8RB32
ChainResidueDetails
AHIS78
BHIS78

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.9, ECO:0007744|PDB:1T8Q, ECO:0007744|PDB:1YDY
ChainResidueDetails
AGLU63
AASP65
AGLU171
BGLU63
BASP65
BGLU171

224572

PDB entries from 2024-09-04

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