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3EIA

Crystal structure of K270Q variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana complexed with L-Glu: External aldimine form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009507cellular_componentchloroplast
A0009570cellular_componentchloroplast stroma
A0009862biological_processsystemic acquired resistance, salicylic acid mediated signaling pathway
A0010285molecular_functionL,L-diaminopimelate aminotransferase activity
A0030170molecular_functionpyridoxal phosphate binding
B0005507molecular_functioncopper ion binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009507cellular_componentchloroplast
B0009570cellular_componentchloroplast stroma
B0009862biological_processsystemic acquired resistance, salicylic acid mediated signaling pathway
B0010285molecular_functionL,L-diaminopimelate aminotransferase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PL6 B 433
ChainResidue
ATYR94
BTYR152
BCYS205
BASN209
BASP237
BTYR240
BSER267
BSER269
BARG278
BTYR364
BARG404
AASN309
BHOH557
BTYR37
BPHE39
BILE63
BGLY64
BGLY127
BALA128
BLYS129

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 433
ChainResidue
ALYS101
AARG104
AASP119
AASP120

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PL6 A 434
ChainResidue
ATYR37
APHE39
AILE63
AGLY64
AGLY127
AALA128
ALYS129
ATYR152
ACYS205
AASN209
AASP237
ATYR240
ASER267
ASER269
AARG278
AARG404
BTYR94
BASN309

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 434
ChainResidue
BLYS101
BARG104
BASP119
BASP120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18952095
ChainResidueDetails
ATYR37
BTYR37

site_idSWS_FT_FI2
Number of Residues22
DetailsBINDING: BINDING => ECO:0000269|PubMed:17583737, ECO:0000269|PubMed:18952095
ChainResidueDetails
AGLY64
AASN309
AARG404
BGLY64
BTYR94
BALA128
BLYS129
BTYR152
BASN209
BTYR240
BSER267
ATYR94
BARG278
BASN309
BARG404
AALA128
ALYS129
ATYR152
AASN209
ATYR240
ASER267
AARG278

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18952095, ECO:0000305|PubMed:17583737
ChainResidueDetails
AGLN270
BGLN270

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cs1
ChainResidueDetails
ATYR152
AASP237

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cs1
ChainResidueDetails
BTYR152
BASP237

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1cs1
ChainResidueDetails
AGLY93

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1cs1
ChainResidueDetails
BGLY93

223790

PDB entries from 2024-08-14

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