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4WYC

Crystal structure of 7,8-diaminopelargonic acid synthase (BioA) from Mycobacterium tuberculosis, complexed with a thiazole benzamide inhibitor

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 Residues19
Detailsbinding site for residue PLP A 501
ChainResidue
ASER123
AALA257
ALYS283
AHOH699
AHOH701
AHOH721
AHOH731
AHOH744
AHOH827
BPRO317
BTHR318
AGLY124
ASER125
ATYR157
AHIS158
AGLY159
AGLU220
AASP254
AILE256

site_idAC2
Number of Residues9
Detailsbinding site for residue 3VS A 502
ChainResidue
APRO24
ATYR25
ATRP64
ATYR157
ASO4505
BGLY93
BGLY316
BPRO317
BTHR318

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 503
ChainResidue
ATHR111
APRO112
AALA113
AASP270
AHOH714
AHOH737
AHOH864

site_idAC4
Number of Residues6
Detailsbinding site for residue FOR A 504
ChainResidue
ALEU290
ASER291
AHOH784
BLEU290
BSER291
BHOH762

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 A 505
ChainResidue
APRO24
AARG400
A3VS502
AHOH767
AHOH792
AHOH960
BGLY93

site_idAC6
Number of Residues10
Detailsbinding site for residue 3VS B 502
ChainResidue
AMET91
AGLY93
AGLY316
APRO317
ATHR318
BPRO24
BTYR25
BTRP64
BHOH848
BHOH931

site_idAC7
Number of Residues1
Detailsbinding site for residue MG B 503
ChainResidue
BTRP45

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO B 504
ChainResidue
AHIS171
BARG50
BHOH603
BHOH842

site_idAC9
Number of Residues24
Detailsbinding site for Di-peptide PLP B 501 and LYS B 283
ChainResidue
APRO317
ATHR318
APHE319
AHOH709
BTRP64
BTRP65
BTHR66
BGLY124
BSER125
BTYR157
BHIS158
BGLU220
BASP254
BILE256
BALA257
BGLY282
BALA284
BLEU285
BHOH682
BHOH723
BHOH729
BHOH788
BHOH833
BHOH845

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

243083

PDB entries from 2025-10-15

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