Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1TUF

Crystal structure of Diaminopimelate Decarboxylase from m. jannaschi

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008652biological_processamino acid biosynthetic process
A0008836molecular_functiondiaminopimelate decarboxylase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0008652biological_processamino acid biosynthetic process
B0008836molecular_functiondiaminopimelate decarboxylase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0016829molecular_functionlyase activity
B0016831molecular_functioncarboxy-lyase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AZ1 A 502
ChainResidue
ALLP83
BSER374
BTYR409
AHIS224
AGLY226
ASER227
AARG307
AARG343
ATYR347
AHOH532
BGLU373

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE AZ1 B 503
ChainResidue
ACYS372
AGLU373
BSER227
BARG307
BARG343
BTYR347

Functional Information from PROSITE/UniProt
site_idPS00878
Number of Residues19
DetailsODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAyKANanlaITrlLaklG
ChainResidueDetails
ATYR80-GLY98

site_idPS00879
Number of Residues14
DetailsODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Gie....IeDVNLGGGLG
ChainResidueDetails
AGLY253-GLY266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_02120","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12429091","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02120","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12429091","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12429091","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02120","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"12429091","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ALLP83
ALYS193

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
BLLP83
BLYS193

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
AHIS224
AGLU304

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
BHIS224
BGLU304

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon