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2CIN

Lysine aminotransferase from M. tuberculosis in the internal aldimine form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003867molecular_functionobsolete 4-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 A1450
ChainResidue
AGLY128
ATHR330
AHOH2207
AHOH2208
AHOH2209
AHOH2210
AHOH2211
AALA129
APHE167
AHIS168
AGLU238
AASP271
AVAL273
AGLN274
ALYS300

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

226707

PDB entries from 2024-10-30

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