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5IE3

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 Residues21
Detailsbinding site for residue AMP A 601
ChainResidue
ASER171
AVAL337
AASP394
ALEU406
AARG409
ALYS500
AOXD602
AHOH707
AHOH713
AHOH718
AHOH860
ASER289
AHOH895
AHOH930
AALA290
ASER291
AGLU310
AALA311
AALA313
AMET314
ATHR315

site_idAC2
Number of Residues9
Detailsbinding site for residue OXD A 602
ChainResidue
AVAL215
AHIS216
ASER289
AALA313
AMET314
ATHR315
AHIS319
ALYS500
AAMP601

site_idAC3
Number of Residues22
Detailsbinding site for residue AMP B 601
ChainResidue
BSER171
BSER289
BALA290
BSER291
BGLU310
BALA311
BALA313
BMET314
BTHR315
BVAL337
BASP394
BLEU406
BARG409
BLYS500
BOXD602
BHOH709
BHOH717
BHOH727
BHOH831
BHOH836
BHOH914
BHOH934

site_idAC4
Number of Residues9
Detailsbinding site for residue OXD B 602
ChainResidue
BVAL215
BHIS216
BSER289
BALA313
BMET314
BTHR315
BHIS319
BLYS500
BAMP601

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
BTHR315
BASP394
ATHR170
AGLU310
ATHR315
AASP394
BTHR170
BGLU310

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

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
AHIS319
ALYS500
BSER289
BMET314
BHIS319
BLYS500
ASER289
AMET314

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

219869

PDB entries from 2024-05-15

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