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

4CXQ

Mycobaterium tuberculosis transaminase BioA complexed with substrate KAPA

Replaces:  4MQN
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 PLP A 501
ChainResidue
ATRP65
AALA257
ALYS283
AKAP502
AHOH2104
AHOH2105
AHOH2107
AHOH2196
BGLY316
BPRO317
BTHR318
AGLY124
ASER125
ATYR157
AHIS158
AGLY159
AGLU220
AASP254
AILE256

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE KAP A 502
ChainResidue
ATYR25
ATRP64
ATYR157
AALA226
ALYS283
AARG400
APLP501
AHOH2032
AHOH2291
AHOH2305
BGLY316
BTHR318

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 503
ChainResidue
AARG193
AHIS232
APRO234
AHOH2306

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AVAL181
AHOH2307
AHOH2308

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
ASER34
APRO35
AVAL36
AHOH2016

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP B 501
ChainResidue
APRO317
ATHR318
AHOH2103
AHOH2232
BTRP65
BGLY124
BSER125
BTYR157
BHIS158
BGLY159
BGLU220
BASP254
BILE256
BALA257
BLYS283
BKAP502
BHOH2070
BHOH2138

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE KAP B 502
ChainResidue
AGLY316
ATHR318
BTYR25
BTRP64
BTYR157
BALA226
BLYS283
BARG400
BPLP501
BHOH2028

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 503
ChainResidue
BVAL222
BHIS232
BHOH2216
BHOH2217

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 504
ChainResidue
AHOH2137
AHOH2308
BVAL181
BHOH2218

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon