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6Q1Q

A hypothetical aminotransferase from Mycobacterium tuberculosis, apo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008360biological_processregulation of cell shape
A0008483molecular_functiontransaminase activity
A0008696molecular_function4-amino-4-deoxychorismate lyase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0030170molecular_functionpyridoxal phosphate binding
A0046394biological_processcarboxylic acid biosynthetic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008360biological_processregulation of cell shape
B0008483molecular_functiontransaminase activity
B0008696molecular_function4-amino-4-deoxychorismate lyase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016829molecular_functionlyase activity
B0019752biological_processcarboxylic acid metabolic process
B0030170molecular_functionpyridoxal phosphate binding
B0046394biological_processcarboxylic acid biosynthetic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue CIT A 301
ChainResidue
APHE31
AHOH409
AHOH419
AHOH496
BARG26
ATHR33
AARG90
AARG115
AARG185
ASER252
AMET254
ATHR255
AEDO305

site_idAC2
Number of Residues5
Detailsbinding site for residue CIT A 302
ChainResidue
ALEU65
APRO66
AARG69
AARG238
AHOH493

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 303
ChainResidue
AARG37
AASP282
AVAL286

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 304
ChainResidue
ATYR179
ATYR210
AALA236

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 305
ChainResidue
ASER252
ASER253
ACIT301
AHOH443
AHOH445
AHOH455

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO B 301
ChainResidue
BALA148
BLYS149
BTHR150
BSER152
BTYR153
BHOH409

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1R, ECO:0007744|PDB:6Q1S
ChainResidueDetails
AARG50
BSER253
ATYR153
ATHR216
ATHR217
ASER253
BARG50
BTYR153
BTHR216
BTHR217

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1S
ChainResidueDetails
ASER252
AMET254
ATHR255
BSER252
BMET254
BTHR255

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for dual ACDL/DAAT activities => ECO:0000305|PubMed:33950161
ChainResidueDetails
AARG26
BARG26

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1R
ChainResidueDetails
ALYS149
BLYS149

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PDB entries from 2024-07-10

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