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2R5E

Aedes kynurenine aminotransferase in complex with glutamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0030170molecular_functionpyridoxal phosphate binding
A0047315molecular_functionkynurenine-glyoxylate transaminase activity
A0097053biological_processL-kynurenine catabolic process
B0005739cellular_componentmitochondrion
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0030170molecular_functionpyridoxal phosphate binding
B0047315molecular_functionkynurenine-glyoxylate transaminase activity
B0097053biological_processL-kynurenine catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE QLP A 430
ChainResidue
ATRP27
AASP221
ATYR224
ASER252
ALYS255
ALYS263
APHE347
AARG405
AHOH434
AHOH457
BTYR73
AGLN44
BTYR286
AGLY45
AGLY109
AALA110
ATYR111
APHE135
AASN189
AASN193

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE QLP B 430
ChainResidue
ATYR73
ATYR286
BTRP27
BGLN44
BGLY45
BGLY109
BALA110
BTYR111
BPHE135
BASN189
BASN193
BASP221
BTYR224
BSER252
BLYS255
BLYS263
BPHE347
BARG405
BHOH646
BHOH844
BHOH855

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15853804, ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY, ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E
ChainResidueDetails
ATYR73
BTYR73

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: in other chain => ECO:0000269|PubMed:15853804, ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY, ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E
ChainResidueDetails
AALA110
BLYS263
AASN193
ATYR224
ASER252
ALYS263
BALA110
BASN193
BTYR224
BSER252

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18186649, ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E
ChainResidueDetails
AARG405
BARG405

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15853804, ECO:0000312|PDB:1YIY
ChainResidueDetails
ALYS255
BLYS255

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN6
AASN157
BASN6
BASN157

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP221
APHE135
ALYS255

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR224
BLYS255

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AARG81

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BARG81

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP221
BPHE135
BLYS255

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP221
APHE135

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP221
BPHE135

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR111
AASP221
ALYS255

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR111
BASP221
BLYS255

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP221
ATYR138
ALYS255

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP221
BTYR138
BLYS255

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR224
ALYS255

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PDB entries from 2024-07-17

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