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4MQQ

Mycobaterium tuberculosis transaminase BioA complexed with benzo[d]thiazole-2-carbohydrazide

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 Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 501
ChainResidue
AHIS271
AEDO502
AHOH785

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
AARG193
AHIS232
AEDO501
AHOH784

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AARG400
A2B6505

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AARG344
AILE413
ACYS414
ATHR415
APRO416
AHOH764
AHOH839

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 2B6 A 505
ChainResidue
ATYR25
ATRP64
ATRP65
AGLY124
ASER125
ATYR157
AHIS158
AGLY159
AASP254
AILE256
ALYS283
ACL503
AHOH624
AHOH632
AHOH677
AHOH722
AHOH767
BPRO317
BTHR318
BHOH639

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE IMD A 506
ChainResidue
AMET165
ACYS168
APRO170
AHIS175
ATHR179
ALEU182
AHOH923
AHOH941

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 2B6 B 501
ChainResidue
AGLY316
APRO317
ATHR318
AHOH631
BPRO24
BTRP64
BGLY124
BSER125
BTYR157
BHIS158
BGLY159
BASP254
BILE256
BLYS283
BARG400
BHOH601
BHOH616
BHOH665
BHOH719

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
BHIS232
BHOH740
BHOH823
BHOH824

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

244349

PDB entries from 2025-11-05

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