Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4W1V

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

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
A3GS502
AHOH643
AHOH648
AHOH650
AHOH686
AHOH698
BPRO317
BTHR318
ASER125
ATYR157
AHIS158
AGLY159
AGLU220
AASP254
AILE256
AALA257

site_idAC2
Number of Residues13
Detailsbinding site for residue 3GS A 502
ChainResidue
APRO24
ATYR25
ATRP64
ATYR157
AARG400
APHE402
APLP501
AHOH686
BMET91
BGLY93
BGLY316
BPRO317
BTHR318

site_idAC3
Number of Residues4
Detailsbinding site for residue PEG A 503
ChainResidue
AHIS232
APRO234
AHIS271
AHOH733

site_idAC4
Number of Residues16
Detailsbinding site for residue PLP B 501
ChainResidue
ATHR318
AHOH644
BGLY124
BSER125
BTYR157
BHIS158
BGLU220
BASP254
BILE256
BALA257
BLYS283
B3GS502
BHOH659
BHOH662
BHOH666
BHOH674

site_idAC5
Number of Residues13
Detailsbinding site for residue 3GS B 502
ChainResidue
AMET91
APHE92
AGLY93
AGLY316
APRO317
ATHR318
BPRO24
BTYR25
BTRP64
BTYR157
BARG400
BPLP501
BHOH662

site_idAC6
Number of Residues8
Detailsbinding site for residue EDO B 503
ChainResidue
BTHR152
BTRP153
BGLY156
BHIS158
BILE167
BVAL219
BGLU220
BGLN224

site_idAC7
Number of Residues1
Detailsbinding site for residue EDO B 505
ChainResidue
BVAL222

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO B 506
ChainResidue
BLEU337
BGLN339
BASP340

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO B 507
ChainResidue
AHIS271
BARG246
BTYR247
BHOH601

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:0000250
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:0000250
ChainResidueDetails
ATYR25
BTYR25

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS283
BLYS283

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon