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4NUR

Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0018741molecular_functionlinear primary-alkylsulfatase activity
A0018909biological_processdodecyl sulfate metabolic process
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0046983molecular_functionprotein dimerization activity
B0016787molecular_functionhydrolase activity
B0018741molecular_functionlinear primary-alkylsulfatase activity
B0018909biological_processdodecyl sulfate metabolic process
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0046983molecular_functionprotein dimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
AASP196
AHIS197
AGLU322
AHIS367
AHOH809
AHOH1444

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 702
ChainResidue
BHOH835
BHOH841
BHOH962
APRO674
AHOH870
AHOH891

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 701
ChainResidue
BASP196
BHIS197
BGLU322
BHIS367
BHOH806

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 702
ChainResidue
AHOH827
AHOH831
AHOH909
BPRO674
BHOH803
BHOH810
BHOH1388

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9I5I9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28442601","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NUR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P32717","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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