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5IE0

Crystal structure of a plant enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006952biological_processdefense response
A0009506cellular_componentplasmodesma
A0009507cellular_componentchloroplast
A0009570cellular_componentchloroplast stroma
A0010030biological_processpositive regulation of seed germination
A0010214biological_processseed coat development
A0016874molecular_functionligase activity
A0033611biological_processoxalate catabolic process
A0048046cellular_componentapoplast
A0050203molecular_functionoxalate-CoA ligase activity
A0050832biological_processdefense response to fungus
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006952biological_processdefense response
B0009506cellular_componentplasmodesma
B0009507cellular_componentchloroplast
B0009570cellular_componentchloroplast stroma
B0010030biological_processpositive regulation of seed germination
B0010214biological_processseed coat development
B0016874molecular_functionligase activity
B0033611biological_processoxalate catabolic process
B0048046cellular_componentapoplast
B0050203molecular_functionoxalate-CoA ligase activity
B0050832biological_processdefense response to fungus
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue SRT A 1001
ChainResidue
AHIS214
AHOH1146
AHOH1164
AHOH1383
AHOH1387
AVAL215
AHIS216
ASER289
AALA313
AMET314
ATHR315
AHIS319
ALYS500

site_idAC2
Number of Residues11
Detailsbinding site for residue SRT A 1002
ChainResidue
AARG20
AARG21
ASER205
AASN253
AHOH1121
AHOH1178
AHOH1272
AHOH1372
AHOH1403
BASP162
BHOH797

site_idAC3
Number of Residues14
Detailsbinding site for residue SRT B 601
ChainResidue
BHIS214
BVAL215
BHIS216
BSER289
BALA313
BMET314
BTHR315
BHIS319
BLYS500
BHOH720
BHOH802
BHOH893
BHOH980
BHOH990

site_idAC4
Number of Residues13
Detailsbinding site for residue SRT B 602
ChainResidue
AASP162
AHOH1607
BARG20
BARG21
BSER205
BASN253
BHOH701
BHOH707
BHOH717
BHOH778
BHOH842
BHOH880
BHOH975

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. FLHTSGTTSrPK
ChainResidueDetails
APHE167-LYS178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27326693, ECO:0007744|PDB:5IE2, ECO:0007744|PDB:5IE3
ChainResidueDetails
ATHR170
AGLU310
ATHR315
AASP394
BTHR170
BGLU310
BTHR315
BASP394

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27326693, ECO:0007744|PDB:5IE2
ChainResidueDetails
AHIS214
AARG409
BHIS214
BARG409

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O24146
ChainResidueDetails
AARG239
AGLY418
BARG239
BGLY418

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27326693, ECO:0007744|PDB:5IE3
ChainResidueDetails
ASER289
AMET314
AHIS319
ALYS500
BSER289
BMET314
BHIS319
BLYS500

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1
BMET1

221371

PDB entries from 2024-06-19

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