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1GCK

THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0033853molecular_functionaspartate-prephenate aminotransferase activity
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B0033853molecular_functionaspartate-prephenate aminotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ASP A 414
ChainResidue
AGLY39
ATRP125
AASN175
ALYS234
AARG361
APLP413
BTYR564
BARG761

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ASP B 914
ChainResidue
BTHR516
BGLY539
BTRP625
BASN675
BLYS734
BTYR822
BARG861
BPLP913
AARG261

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 413
ChainResidue
AGLY100
ASER101
ATRP125
ATYR128
AASN171
AASN175
AASP203
AILE205
ATYR206
AALA233
ALYS234
AARG242
AASP414
BTYR564

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP B 913
ChainResidue
ATYR64
BGLY599
BGLY600
BSER601
BTRP625
BASN675
BASP703
BILE705
BTYR706
BLYS734
BARG742
BASP914

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GAAKafAMtGWRIG
ChainResidueDetails
AGLY231-GLY244

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00509
ChainResidueDetails
AGLY39
BGLY539

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:1GCK
ChainResidueDetails
ATRP125
AASN175
AARG361
BTRP625
BASN675
BARG861

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275
ChainResidueDetails
ALYS12
BLYS512

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4
ChainResidueDetails
ALYS234
BLYS734

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR124
AASP203

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BALA568

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR624
BASP703

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AALA68

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS234
ATRP125
AASP203

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BLYS734
BTRP625
BASP703

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS234
ATYR124
AASP203

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BLYS734
BTYR624
BASP703

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP125
AASP203

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP625
BASP703

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS234
AASP203
ATYR128

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BLYS734
BTYR628
BASP703

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PDB entries from 2024-05-01

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