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4XJO

Crystal structure of 7,8-diaminopelargonic acid synthase (BioA) from Mycobacterium tuberculosis, complexed with an inhibitor optimized from HTS lead

Functional Information from GO Data
ChainGOidnamespacecontents
A0004015molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0009102biological_processbiotin biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0004015molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0009102biological_processbiotin biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue PLP A 501
ChainResidue
AGLY124
ALYS283
AHOH658
AHOH665
AHOH777
AHOH823
BPRO317
BTHR318
BHOH609
BHOH799
ASER125
ATYR157
AHIS158
AGLY159
AGLU220
AASP254
AILE256
AALA257

site_idAC2
Number of Residues16
Detailsbinding site for residue 41O A 502
ChainResidue
ATYR25
ATRP64
AGLY156
ATYR157
AGLY172
AGLY173
AALA226
AARG400
AARG403
AHOH621
BMET91
BPHE92
BGLY93
BGLY316
BPRO317
BTHR318

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 503
ChainResidue
AARG344
AILE413
ACYS414
ATHR415
APRO416

site_idAC4
Number of Residues17
Detailsbinding site for residue PLP B 501
ChainResidue
APRO317
ATHR318
AHOH607
BGLY124
BSER125
BTYR157
BHIS158
BGLU220
BASP254
BILE256
BALA257
BLYS283
BHOH630
BHOH647
BHOH702
BHOH708
BHOH804

site_idAC5
Number of Residues14
Detailsbinding site for residue 41O B 502
ChainResidue
AMET91
APHE92
AGLY93
AGLY316
APRO317
ATHR318
BPRO24
BTYR25
BTRP64
BGLY156
BTYR157
BGLY172
BGLY173
BALA226

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 B 503
ChainResidue
BTRP139
BCYS244
BGLU248
BVAL249
BLEU250
BHOH637

site_idAC7
Number of Residues5
Detailsbinding site for residue CL B 504
ChainResidue
AGLY355
ATHR423
ASER424
AHOH897
AHOH923

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: BINDING => ECO:0000269|PubMed:20565114
ChainResidueDetails
ATRP64
ATYR157
AGLY316
BTRP64
BTYR157
BGLY316

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00834
ChainResidueDetails
AGLY124
AASP254
ALYS283
APRO317
BGLY124
BASP254
BLYS283
BPRO317

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:20565114
ChainResidueDetails
AARG400
BARG400

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000305|PubMed:20565114
ChainResidueDetails
ATYR25
BTYR25

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20565114, ECO:0007744|PDB:3BV0, ECO:0007744|PDB:3LV2
ChainResidueDetails
ALYS283
BLYS283

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PDB entries from 2024-11-06

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