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7PTH

C54S mutant of choline-sulfatase from E. meliloti CECT4857 bound to choline

Functional Information from GO Data
ChainGOidnamespacecontents
A0004423molecular_functioniduronate-2-sulfatase activity
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0042425biological_processcholine biosynthetic process
A0046872molecular_functionmetal ion binding
A0047753molecular_functioncholine-sulfatase activity
B0004423molecular_functioniduronate-2-sulfatase activity
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0042425biological_processcholine biosynthetic process
B0046872molecular_functionmetal ion binding
B0047753molecular_functioncholine-sulfatase activity
C0004423molecular_functioniduronate-2-sulfatase activity
C0005737cellular_componentcytoplasm
C0016787molecular_functionhydrolase activity
C0042425biological_processcholine biosynthetic process
C0046872molecular_functionmetal ion binding
C0047753molecular_functioncholine-sulfatase activity
D0004423molecular_functioniduronate-2-sulfatase activity
D0005737cellular_componentcytoplasm
D0016787molecular_functionhydrolase activity
D0042425biological_processcholine biosynthetic process
D0046872molecular_functionmetal ion binding
D0047753molecular_functioncholine-sulfatase activity
Functional Information from PROSITE/UniProt
site_idPS00149
Number of Residues11
DetailsSULFATASE_2 Sulfatases signature 2. GYyTalSGK.MH
ChainResidueDetails
AGLY94-HIS104

site_idPS00523
Number of Residues13
DetailsSULFATASE_1 Sulfatases signature 1. PLSAPARasFMAG
ChainResidueDetails
APRO52-GLY64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P15289
ChainResidueDetails
ASER54
BSER54
CSER54
DSER54

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P15289
ChainResidueDetails
AHIS104
BHIS104
CHIS104
DHIS104

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP14
AGLN15
AASP296
AHIS297
BASP14
BGLN15
BASP296
BHIS297
CASP14
CGLN15
CASP296
CHIS297
DASP14
DGLN15
DASP296
DHIS297

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: via 3-oxoalanine => ECO:0000250
ChainResidueDetails
ASER54
BSER54
CSER54
DSER54

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: 3-oxoalanine (Cys) => ECO:0000250|UniProtKB:P15289
ChainResidueDetails
ASER54
BSER54
CSER54
DSER54

219869

PDB entries from 2024-05-15

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