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1LC8

Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica complexed with its reaction intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0009058biological_processbiosynthetic process
A0009236biological_processcobalamin biosynthetic process
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0048472molecular_functionthreonine-phosphate decarboxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 33P A 800
ChainResidue
AHIS8
AASP185
AALA187
APHE188
ASER213
ATHR215
ALYS216
AARG224
AARG323
ATYR328
AARG337
AGLY9
AHOH1014
AHOH1028
ATYR56
AGLY84
AGLU85
ATHR86
APHE108
ACYS153
AASN157

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLTKfyAIpGLRLG
ChainResidueDetails
ASER213-GLY226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12119022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LC7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"11939774","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LKC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP185
APHE108

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AARG55

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS216
AASP185
APHE108

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS216
AHIS194

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PDB entries from 2025-10-08

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