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4CXR

Mycobaterium tuberculosis transaminase BioA complexed with 1-(1,3- benzothiazol-2-yl)methanamine

Replaces:  4MQO
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
A2BG502
AHOH2051
AHOH2053
AHOH2055
AHOH2090
BGLY316
BPRO317
BTHR318
ASER125
ATYR157
AHIS158
AGLU220
AASP254
AILE256
AALA257
ALYS283

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 2BG A 502
ChainResidue
ATYR25
ATRP64
ATRP65
ATYR157
AALA226
APLP501
BGLY316
BTHR318

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
ATYR25
ATRP64
AARG400
AHOH2007
AHOH2133
AHOH2141
BGLY93

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
ATRP139
AARG142
ALEU144
ALYS147
AGLU248
BARG154

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP B 501
ChainResidue
APRO317
ATHR318
AHOH2049
AHOH2111
BGLY124
BSER125
BTYR157
BHIS158
BGLY159
BGLU220
BASP254
BILE256
BALA257
BLYS283
BHOH2026
BHOH2027
BHOH2060

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
AGLY93
AGLY94
BTRP64
BARG400
BHOH2003

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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