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1HKW

MYCOBACTERIUM DIAMINOPIMELATE DICARBOXYLASE (LysA)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0008836molecular_functiondiaminopimelate decarboxylase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009274cellular_componentpeptidoglycan-based cell wall
A0016830molecular_functioncarbon-carbon lyase activity
A0016831molecular_functioncarboxy-lyase activity
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0008836molecular_functiondiaminopimelate decarboxylase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009274cellular_componentpeptidoglycan-based cell wall
B0016830molecular_functioncarbon-carbon lyase activity
B0016831molecular_functioncarboxy-lyase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
AGLY258
APRO301
AGLY302
AARG303
ATYR405
AHOH2121

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BARG303
BTYR405
BHOH2093
BGLY258
BPRO301
BGLY302

Functional Information from PROSITE/UniProt
site_idPS00878
Number of Residues19
DetailsODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAaKAFlcseVArwIseeG
ChainResidueDetails
ATYR69-GLY87

site_idPS00879
Number of Residues18
DetailsODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. GpektaqIaTVDLGGGLG
ChainResidueDetails
AGLY243-GLY260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02120
ChainResidueDetails
ACYS375
BCYS375

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|PubMed:12637582
ChainResidueDetails
ASER216
BTYR405
AARG303
AARG344
AGLU376
ATYR405
BSER216
BARG303
BARG344
BGLU376

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12637582
ChainResidueDetails
AGLY258
BGLY258

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02120, ECO:0000269|PubMed:12637582
ChainResidueDetails
AGLU300
BGLU300

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02120
ChainResidueDetails
ATYR348
BTYR348

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:12637582
ChainResidueDetails
ALYS72
BLYS72

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ALYS182
ALYS72
BCYS375
BHIS329

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ACYS375
AHIS329
BLYS182
BLYS72

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
AGLU300
AHIS213
ALYS72

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
BGLU300
BHIS213
BLYS72

224201

PDB entries from 2024-08-28

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