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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
AHOH733
AHOH755
AHOH764
AHOH774
AHOH872
BPRO317
BTHR318
BHOH688
ASER125
ATYR157
AHIS158
AGLY159
AGLU220
AASP254
AILE256
AALA257

site_idAC2
Number of Residues19
Detailsbinding site for residue 41N A 502
ChainResidue
ATYR25
ATRP64
AGLY156
ATYR157
ACYS168
AGLY172
AGLY173
AALA226
AGLY227
AARG400
APHE402
AHOH779
AHOH798
BMET91
BPHE92
BGLY93
BGLY316
BPRO317
BTHR318

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 503
ChainResidue
ALEU385
APHE402
AARG403
AHOH815
AHOH893
AHOH1022

site_idAC4
Number of Residues7
Detailsbinding site for residue PEG A 504
ChainResidue
AARG193
AVAL222
AHIS232
AASP233
APRO234
AHOH1066
AHOH1067

site_idAC5
Number of Residues19
Detailsbinding site for residue 41N B 502
ChainResidue
AMET91
APHE92
AGLY93
AGLY316
APRO317
ATHR318
BTYR25
BTRP64
BGLY156
BTYR157
BCYS168
BGLY172
BGLY173
BALA226
BGLY227
BARG400
BPHE402
BHOH773
BHOH920

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO B 503
ChainResidue
BGLU56
BHOH610

site_idAC7
Number of Residues9
Detailsbinding site for residue EDO B 504
ChainResidue
AASP122
APHE319
AHOH737
BASP122
BSER123
BGLY282
BSER291
BLEU292
BHOH798

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO B 505
ChainResidue
BGLY355
BTHR358
BTHR420
BTHR423
BSER424

site_idAC9
Number of Residues5
Detailsbinding site for residue PEG B 506
ChainResidue
BARG193
BHIS232
BASP233
BPRO234
BHIS271

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO B 507
ChainResidue
AHIS271
AALA272
BARG246
BTYR247

site_idAD2
Number of Residues23
Detailsbinding site for Di-peptide PLP B 501 and LYS B 283
ChainResidue
BTHR66
BGLY124
BSER125
BTYR157
BHIS158
BGLY159
BGLU220
BASP254
BILE256
BALA257
BGLY282
BALA284
BLEU285
BHOH710
BHOH720
BHOH725
BHOH749
BHOH798
APRO317
ATHR318
AHOH737
BTRP64
BTRP65

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 2024-07-24

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