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

1RLO

Phospho-aspartyl Intermediate Analogue of ybiV from E. coli K12

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005829cellular_componentcytosol
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0046872molecular_functionmetal ion binding
A0050286molecular_functionsorbitol-6-phosphatase activity
A0050308molecular_functionsugar-phosphatase activity
A0103026molecular_functionfructose-1-phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0005829cellular_componentcytosol
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0046872molecular_functionmetal ion binding
B0050286molecular_functionsorbitol-6-phosphatase activity
B0050308molecular_functionsugar-phosphatase activity
B0103026molecular_functionfructose-1-phosphatase activity
C0000287molecular_functionmagnesium ion binding
C0005829cellular_componentcytosol
C0016787molecular_functionhydrolase activity
C0016791molecular_functionphosphatase activity
C0046872molecular_functionmetal ion binding
C0050286molecular_functionsorbitol-6-phosphatase activity
C0050308molecular_functionsugar-phosphatase activity
C0103026molecular_functionfructose-1-phosphatase activity
D0000287molecular_functionmagnesium ion binding
D0005829cellular_componentcytosol
D0016787molecular_functionhydrolase activity
D0016791molecular_functionphosphatase activity
D0046872molecular_functionmetal ion binding
D0050286molecular_functionsorbitol-6-phosphatase activity
D0050308molecular_functionsugar-phosphatase activity
D0103026molecular_functionfructose-1-phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 801
ChainResidue
ABFD9
AASP11
AASP215
AHOH802
AHOH927

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 802
ChainResidue
BHOH899
BBFD9
BASP11
BASP215
BHOH805

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 803
ChainResidue
CBFD9
CASP11
CASP215
CHOH891
CHOH912

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 804
ChainResidue
DBFD9
DASP11
DASP215
DHOH895
DHOH896

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 805
ChainResidue
CGLY45
CASN46
CTYR130
CSER150
CSER178
CPHE182
CASP184
CHOH875

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 806
ChainResidue
DGLY45
DTYR130
DSER150
DSER178
DPHE182
DASP184
DHOH840

Functional Information from PROSITE/UniProt
site_idPS01229
Number of Residues23
DetailsCOF_2 Hypothetical cof family signature 2. IGDSgNDaemLkmArySfaMgnA
ChainResidueDetails
AILE213-ALA235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255
ChainResidueDetails
ABFD9
BBFD9
CBFD9
DBFD9

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING:
ChainResidueDetails
ABFD9
BASP11
BSER44
BLYS192
BASP215
BSER216
CBFD9
CMET10
CASP11
CSER44
CLYS192
AMET10
CASP215
CSER216
DBFD9
DMET10
DASP11
DSER44
DLYS192
DASP215
DSER216
AASP11
ASER44
ALYS192
AASP215
ASER216
BBFD9
BMET10

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN218
BASN218
CASN218
DASN218

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon