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3EI7

Crystal structure of apo-LL-diaminopimelate aminotransferase from Arabidopsis thaliana (no PLP)

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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 433
ChainResidue
AALA35
AGLY36
ATYR37
APRO40
AARG44

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 433
ChainResidue
BPRO40
BARG44
AARG302
BALA35
BGLY36
BTYR37

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
ALYS270
BLYS270

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR152
AASP237
ALYS270

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BGLY93

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR152
BASP237
BLYS270

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP237
APHE139
ALYS270

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP237
BPHE139
BLYS270

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP237
ALYS270
APHE168

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP237
BLYS270
BPHE168

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR152
AASP237

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR152
BASP237

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AGLY93

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PDB entries from 2024-07-24

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