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3STP

Crystal structure of a putative galactonate dehydratase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0006091biological_processgeneration of precursor metabolites and energy
A0016052biological_processcarbohydrate catabolic process
A0016836molecular_functionhydro-lyase activity
A0050032molecular_functionL-rhamnonate dehydratase activity
A0140356molecular_functionL-lyxonate dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 391
ChainResidue
AGLU214
AGLU240
AGLU266
AHOH392
AHOH393
AHOH394

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q8ZNF9","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"24831290","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24831290","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3STP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Increases basicity of active site His","evidences":[{"source":"PubMed","id":"24831290","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"Q8ZNF9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

255615

PDB entries from 2026-06-24

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