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5KGS

Crystal structure of 7,8-diaminopelargonic acid synthase (BioA) from Mycobacterium tuberculosis, complexed with an inhibitor optimized from HTS lead: 5-[4-(1,3-benzodioxol-5-ylcarbonyl)piperazin-1-yl]-2,3-dihydroinden-1-one

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 Residues15
Detailsbinding site for residue PLP A 501
ChainResidue
AGLY124
AHOH638
AHOH658
AHOH682
BPRO317
BTHR318
BHOH621
ASER125
ATYR157
AHIS158
AGLU220
AASP254
AILE256
AALA257
ALYS283

site_idAC2
Number of Residues15
Detailsbinding site for residue 6SR A 502
ChainResidue
ATRP64
AGLY156
ATYR157
ACYS168
AGLY172
AGLY173
AALA226
AGLY227
APHE402
BMET91
BPHE92
BGLY93
BGLY316
BPRO317
BTHR318

site_idAC3
Number of Residues6
Detailsbinding site for residue PGE A 503
ChainResidue
AARG193
APHE231
AHIS232
AASP233
APRO234
ACYS371

site_idAC4
Number of Residues16
Detailsbinding site for residue 6SR B 502
ChainResidue
AMET91
APHE92
AGLY93
AGLY316
APRO317
ATHR318
BTYR25
BTRP64
BGLY156
BTYR157
BCYS168
BGLY172
BGLY173
BALA226
BGLY227
BPHE402

site_idAC5
Number of Residues4
Detailsbinding site for residue PGE B 503
ChainResidue
BARG193
BASP233
BPRO234
BHIS271

site_idAC6
Number of Residues22
Detailsbinding site for Di-peptide PLP B 501 and LYS B 283
ChainResidue
APRO317
ATHR318
AHOH601
BTRP64
BTRP65
BTHR66
BGLY124
BSER125
BTYR157
BHIS158
BGLY159
BGLU220
BASP254
BILE256
BALA257
BGLY282
BALA284
BLEU285
BHOH652
BHOH682
BHOH694
BHOH707

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 Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00834
ChainResidueDetails
ATRP64
BGLY124
BTYR157
BASP254
BLYS283
BGLY316
BPRO317
BARG400
AGLY124
ATYR157
AASP254
ALYS283
AGLY316
APRO317
AARG400
BTRP64

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000255|HAMAP-Rule:MF_00834
ChainResidueDetails
ATYR25
BTYR25

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00834
ChainResidueDetails
ALYS283
BLYS283

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PDB entries from 2024-07-24

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