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1LC7

Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica complexed with a substrate

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 Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 800
ChainResidue
ATYR56
AGLY84
AGLU85
ATHR86
ASER213
ATHR215
ALYS216
AARG224
AHOH1052

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TPO A 990
ChainResidue
AALA7
AHIS8
AGLY9
AALA31
AASN32
APHE108
AASN157
APHE188
ALYS216
AARG323
ATYR328
AARG337
AHOH1015

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: BINDING => ECO:0000269|PubMed:12119022, ECO:0007744|PDB:1LC7
ChainResidueDetails
AARG337
AHIS8
AASN32
AASN157
AARG323

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11939774, ECO:0007744|PDB:1LKC
ChainResidueDetails
ALYS216

218500

PDB entries from 2024-04-17

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