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4XEW

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

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 Residues17
Detailsbinding site for residue PLP A 501
ChainResidue
AGLY124
ALYS283
AHOH632
AHOH644
AHOH645
AHOH668
AHOH673
BPRO317
BTHR318
ASER125
ATYR157
AHIS158
AGLY159
AGLU220
AASP254
AILE256
AALA257

site_idAC2
Number of Residues12
Detailsbinding site for residue 40N A 502
ChainResidue
APRO24
ATYR25
ATRP64
ATYR157
AALA226
AARG400
APHE402
AHOH610
BGLY93
BGLY316
BPRO317
BTHR318

site_idAC3
Number of Residues18
Detailsbinding site for residue PLP B 501
ChainResidue
APRO317
ATHR318
AHOH605
BSER123
BGLY124
BSER125
BTYR157
BHIS158
BGLU220
BASP254
BILE256
BALA257
BLYS283
BHOH622
BHOH636
BHOH645
BHOH650
BHOH660

site_idAC4
Number of Residues10
Detailsbinding site for residue 40N B 502
ChainResidue
AGLY93
AGLY316
APRO317
ATHR318
BPRO24
BTYR25
BTRP64
BTYR157
BALA226
BHOH610

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
BTYR157
BGLY316
AGLY316
BTRP64
ATYR157
ATRP64

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

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
BLYS283
ALYS283

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PDB entries from 2024-06-12

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