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4MQR

Mycobaterium tuberculosis transaminase BioA complexed with E)-5-hydroxy-4-(((Z)-isonicotinoyldiazenyl)methylene)-6-methyl-1,4-dihydropyridin-3-yl)methyl phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004015molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0009102biological_processbiotin biosynthetic process
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
B0004015molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0009102biological_processbiotin biosynthetic process
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 2B9 A 501
ChainResidue
ATYR25
AILE256
ALYS283
AHOH622
AHOH644
AHOH667
BGLY316
BPRO317
BTHR318
BHOH631
ATRP64
ASER123
AGLY124
ASER125
ATYR157
AHIS158
AGLY159
AASP254

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
AARG193
APHE231
AASP367
AARG369
AHOH656

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AVAL108
AASP109
ATHR111
AALA113
AHOH688
AHOH740
BARG235

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 2B9 B 501
ChainResidue
AGLY316
APRO317
ATHR318
AHOH603
BTRP64
BGLY124
BSER125
BTYR157
BHIS158
BGLY159
BASP254
BILE256
BLYS283
BHOH609
BHOH648
BHOH655
BHOH761

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
AARG235
AHIS271
AALA272
AHOH712
BARG246
BTYR247

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 503
ChainResidue
ALEU144
AGLY212
AHOH636
BARG154
BPRO189
BHOH616
BHOH644
BHOH749

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEIat.GFgRtGalfaadhagvsp....DIMcvGKaltGG
ChainResidueDetails
ALEU251-GLY288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00834","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM","evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BV0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LV2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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