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8ZKV

Crystal structure of mutant catalytic domains of threonine deaminase in complex with PLP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004794molecular_functionthreonine deaminase activity
A0006520biological_processamino acid metabolic process
A0009097biological_processisoleucine biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0004794molecular_functionthreonine deaminase activity
B0006520biological_processamino acid metabolic process
B0009097biological_processisoleucine biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
C0004794molecular_functionthreonine deaminase activity
C0006520biological_processamino acid metabolic process
C0009097biological_processisoleucine biosynthetic process
C0030170molecular_functionpyridoxal phosphate binding
D0004794molecular_functionthreonine deaminase activity
D0006520biological_processamino acid metabolic process
D0009097biological_processisoleucine biosynthetic process
D0030170molecular_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 Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9562556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
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

site_idMCSA2
Number of Residues2
DetailsM-CSA 886
ChainResidueDetails
BLLP62covalent catalysis, proton shuttle (general acid/base)
BVAL319electrostatic stabiliser

site_idMCSA3
Number of Residues2
DetailsM-CSA 886
ChainResidueDetails
CLLP62covalent catalysis, proton shuttle (general acid/base)
CVAL319electrostatic stabiliser

site_idMCSA4
Number of Residues2
DetailsM-CSA 886
ChainResidueDetails
DLLP62covalent catalysis, proton shuttle (general acid/base)
DVAL319electrostatic stabiliser

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PDB entries from 2025-12-17

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