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4MQP

Mycobaterium tuberculosis transaminase BioA complexed with 2-hydrazinylbenzo[d]thiazole

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 Residues19
DetailsBINDING SITE FOR RESIDUE 2B1 A 501
ChainResidue
ATRP64
AASP254
AILE256
ALYS283
ATYR407
AHOH609
AHOH626
AHOH804
BPRO317
BTHR318
BHOH687
ATRP65
AGLY124
ASER125
ATYR157
AHIS158
AGLY159
AGLU220
AALA226

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
AHIS232
AHOH725
AHOH765
AHOH766

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AGLU56

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 2B1 B 501
ChainResidue
AGLY316
APRO317
ATHR318
BTRP65
BGLY124
BSER125
BTYR157
BHIS158
BGLY159
BGLU220
BALA226
BASP254
BILE256
BLYS283
BPHE402
BTYR407
BHOH603
BHOH613
BHOH628
BHOH634
BHOH684
BHOH695
BHOH724

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
BALA183
BALA184

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 503
ChainResidue
BARG193
BHIS232
BASP233
BHOH723
BHOH765

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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