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9D2Q

Crystal structure of E. coli Threonine dehydratase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004794molecular_functionthreonine deaminase activity
A0006566biological_processthreonine metabolic process
A0008652biological_processamino acid biosynthetic process
A0009066biological_processaspartate family amino acid metabolic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0016597molecular_functionamino acid binding
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Edrqp.VHSFKLRGA
ChainResidueDetails
AGLU53-ALA66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsDomain: {"description":"ACT-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01008","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9562556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"9562556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 886
ChainResidueDetails
ALLP62covalent catalysis, proton shuttle (general acid/base)
AVAL319electrostatic stabiliser

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PDB entries from 2025-10-08

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