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2JJG

Crystal structure of the M. tuberculosis Lysine-epsilon aminotransferase (Rv3290c) complexed to an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003867molecular_function4-aminobutyrate transaminase activity
A0008483molecular_functiontransaminase activity
A0009450biological_processgamma-aminobutyric acid catabolic process
A0017000biological_processantibiotic biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0045484molecular_functionL-lysine 6-transaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 600
ChainResidue
AGLY128
ASER329
ATHR330
AL18601
AHOH2106
AHOH2107
AHOH2108
AALA129
APHE167
AHIS168
AGLU238
AASP271
AVAL273
AGLN274
ALYS300

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE L18 A 601
ChainResidue
AALA129
APHE167
AGLY169
AARG170
ALYS181
AILE184
ASER325
AASN328
ASER329
ATHR330
APLP600

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVqt.GCgLtGtawayqqldvap....DIVafGKktqVC
ChainResidueDetails
ALEU268-CYS305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255
ChainResidueDetails
ALYS300

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d7r
ChainResidueDetails
ALYS300
APHE167
AASP271

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1d7r
ChainResidueDetails
AASP97

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PDB entries from 2024-07-17

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