Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1T8Q

Structural genomics, Crystal structure of Glycerophosphoryl diester phosphodiesterase from E. 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
C0006629biological_processlipid metabolic process
C0008081molecular_functionphosphoric diester hydrolase activity
D0006629biological_processlipid metabolic process
D0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1601
ChainResidue
AGLU63
AASP65
AGLU171
AGOL1605
AHOH1615

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1602
ChainResidue
BHOH1612
BGLU63
BASP65
BGLU171
BGOL1606

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 1603
ChainResidue
CGLU63
CASP65
CGLU171
CGOL1607
CHOH1614

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 1604
ChainResidue
DGLU63
DASP65
DGLU171
DGOL1608
DHOH1616

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 1605
ChainResidue
AHIS36
AARG37
AGLU63
AASP65
AGLU171
ALYS173
ATYR313
AMG1601
AHOH1615
AHOH1616
AHOH1657
AHOH1905

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 1606
ChainResidue
BHIS36
BARG37
BGLU63
BASP65
BGLU171
BLYS173
BPHE210
BMG1602
BHOH1612
BHOH1613
BHOH1677

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL C 1607
ChainResidue
CHIS36
CARG37
CGLU63
CGLU171
CLYS173
CPHE210
CTYR313
CMG1603
CHOH1653
CHOH1739

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL D 1608
ChainResidue
DHIS36
DARG37
DGLU63
DASP65
DGLU171
DLYS173
DPHE210
DMG1604
DHOH1616
DHOH1639
DHOH1746

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1609
ChainResidue
ALYS195
AHOH1811
AHOH1955
AHOH1962

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1610
ChainResidue
BLYS195
BHOH1847
BHOH1870

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 1611
ChainResidue
BLYS140
CLYS195
CTYR196
CHOH1750

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL D 1612
ChainResidue
DLYS195
DTYR196

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 1613
ChainResidue
CARG95
CALA96
CASP106
CHOH1862

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1614
ChainResidue
AARG95
AASP106
AHOH1779
AHOH1909
AHOH1910

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 1615
ChainResidue
DARG95
DARG97
DASP106
DHOH1728
DHOH1736

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q8RB32
ChainResidueDetails
AHIS36
BHIS36
CHIS36
DHIS36

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q8RB32
ChainResidueDetails
AHIS78
BHIS78
CHIS78
DHIS78

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|Ref.9, ECO:0007744|PDB:1T8Q, ECO:0007744|PDB:1YDY
ChainResidueDetails
AGLU63
DGLU63
DASP65
DGLU171
AASP65
AGLU171
BGLU63
BASP65
BGLU171
CGLU63
CASP65
CGLU171

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon