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3CSW

Crystal structure of a putative branched-chain amino acid aminotransferase (TM0831) from Thermotoga maritima at 2.15 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0009098biological_processL-leucine biosynthetic process
A0009099biological_processvaline biosynthetic process
A0019752biological_processcarboxylic acid metabolic process
A0046394biological_processcarboxylic acid biosynthetic process
A0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
A0052654molecular_functionL-leucine transaminase activity
A0052655molecular_functionL-valine transaminase activity
A0052656molecular_functionL-isoleucine transaminase activity
B0003824molecular_functioncatalytic activity
B0008483molecular_functiontransaminase activity
B0008652biological_processamino acid biosynthetic process
B0009082biological_processbranched-chain amino acid biosynthetic process
B0009097biological_processisoleucine biosynthetic process
B0009098biological_processL-leucine biosynthetic process
B0009099biological_processvaline biosynthetic process
B0019752biological_processcarboxylic acid metabolic process
B0046394biological_processcarboxylic acid biosynthetic process
B0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
B0052654molecular_functionL-leucine transaminase activity
B0052655molecular_functionL-valine transaminase activity
B0052656molecular_functionL-isoleucine transaminase activity
C0003824molecular_functioncatalytic activity
C0008483molecular_functiontransaminase activity
C0008652biological_processamino acid biosynthetic process
C0009082biological_processbranched-chain amino acid biosynthetic process
C0009097biological_processisoleucine biosynthetic process
C0009098biological_processL-leucine biosynthetic process
C0009099biological_processvaline biosynthetic process
C0019752biological_processcarboxylic acid metabolic process
C0046394biological_processcarboxylic acid biosynthetic process
C0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
C0052654molecular_functionL-leucine transaminase activity
C0052655molecular_functionL-valine transaminase activity
C0052656molecular_functionL-isoleucine transaminase activity
D0003824molecular_functioncatalytic activity
D0008483molecular_functiontransaminase activity
D0008652biological_processamino acid biosynthetic process
D0009082biological_processbranched-chain amino acid biosynthetic process
D0009097biological_processisoleucine biosynthetic process
D0009098biological_processL-leucine biosynthetic process
D0009099biological_processvaline biosynthetic process
D0019752biological_processcarboxylic acid metabolic process
D0046394biological_processcarboxylic acid biosynthetic process
D0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
D0052654molecular_functionL-leucine transaminase activity
D0052655molecular_functionL-valine transaminase activity
D0052656molecular_functionL-isoleucine transaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 300
ChainResidue
AARG50
AASN169
ALEU188
AGLY190
AILE191
ATHR192
ATHR228
ALYS133
AILE140
AARG144
AGLU164
AGLY165
ASER166
APHE167
ASER168

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP C 300
ChainResidue
CARG50
CLYS133
CGLU164
CSER166
CPHE167
CSER168
CASN169
CLEU188
CGLY190
CILE191
CTHR192
CTHR228

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNL B 276
ChainResidue
BARG85
BHIS227
BTHR228
BSER229

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNL C 301
ChainResidue
CTHR33
CHIS227
CTHR228
CSER229

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNL A 301
ChainResidue
ATHR33
AHIS227
ATHR228
ASER229

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNL D 275
ChainResidue
DTHR33
DARG85
DHIS227
DTHR228
DSER229

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CIT A 302
ChainResidue
ALEU142
AARG145
AGLU146
BPHE57
BPHE58
CASP67
CLYS71

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CIT D 276
ChainResidue
DARG122
DPRO124
DASP125
DLEU126
DASN159

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CIT B 277
ChainResidue
BARG122
BPRO124
BASP125
BLEU126
BLEU158
BASN159

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 303
ChainResidue
AASN159
AASP184
ASER185

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 304
ChainResidue
AASP125
APRO129
BASN119

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD C 303
ChainResidue
CASP184

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD B 278
ChainResidue
BLYS52
BASP56
BASN59
BLEU60
CPHE66

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD B 279
ChainResidue
BASP125
BLEU126
BSER127
BTHR128
BPRO129

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD D 277
ChainResidue
CASN119
DPHE57
DLEU126
DSER127
DTHR128
DPRO129

Functional Information from PROSITE/UniProt
site_idPS00770
Number of Residues30
DetailsAA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSfsNVFlvkegk......LiTpsldsgi.LdGItR
ChainResidueDetails
AGLU164-ARG193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS133
BLYS133
CLYS133
DLYS133

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
ALYS133
AGLU164
ALEU188

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
BLYS133
BGLU164
BLEU188

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
CLYS133
CGLU164
CLEU188

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
DLYS133
DGLU164
DLEU188

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
ALYS133

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
BLYS133

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
CLYS133

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
DLYS133

222036

PDB entries from 2024-07-03

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