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4WYE

Crystal structure of 7,8-diaminopelargonic acid synthase (BioA) from Mycobacterium tuberculosis complexed with a DSF fragment hit

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 Residues16
Detailsbinding site for residue PLP A 501
ChainResidue
AGLY124
ALYS283
AHOH669
AHOH693
AHOH764
BPRO317
BTHR318
BHOH713
ASER125
ATYR157
AHIS158
AGLY159
AGLU220
AASP254
AILE256
AALA257

site_idAC2
Number of Residues11
Detailsbinding site for residue 3VW A 502
ChainResidue
ATYR25
ATRP64
ATRP65
AGLY225
AALA226
AMET229
ALYS283
APHE402
ATYR407
AHOH693
BGLY316

site_idAC3
Number of Residues12
Detailsbinding site for residue EPE A 503
ChainResidue
ATYR25
ASER26
ASER27
AGLU31
ATRP64
AARG400
AHOH699
AHOH710
AHOH806
AHOH840
AHOH872
BGLY93

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 504
ChainResidue
AHIS271
AALA272
AHOH635
BARG246
BTYR247

site_idAC5
Number of Residues9
Detailsbinding site for residue 3VW B 501
ChainResidue
AGLY316
BTYR25
BTRP64
BTRP65
BALA226
BLYS283
BPHE402
BTYR407
BHOH712

site_idAC6
Number of Residues11
Detailsbinding site for residue EPE B 503
ChainResidue
AGLY93
BPRO24
BTYR25
BSER26
BGLU31
BTRP64
BARG400
BHOH722
BHOH734
BHOH735
BHOH762

site_idAC7
Number of Residues7
Detailsbinding site for residue ACN B 504
ChainResidue
BTYR138
BTRP139
BVAL249
BLEU250
BHOH746
BHOH794
BHOH833

site_idAC8
Number of Residues24
Detailsbinding site for Di-peptide PLP B 502 and LYS B 283
ChainResidue
APRO317
ATHR318
APHE319
AHOH668
AHOH698
BTRP64
BTRP65
BTHR66
BGLY124
BSER125
BTYR157
BHIS158
BGLU220
BASP254
BILE256
BALA257
BGLY282
BALA284
BLEU285
B3VW501
BHOH689
BHOH712
BHOH716
BHOH730

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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